source stringlengths 32 209 | text stringlengths 18 1.5k |
|---|---|
https://en.wikipedia.org/wiki/N-methylcoclaurine%203%27-monooxygenase | In enzymology, a N-methylcoclaurine 3'-monooxygenase () is an enzyme that catalyzes the chemical reaction
(S)-N-methylcoclaurine + NADPH + H+ + O2 (S)-3'-hydroxy-N-methylcoclaurine + NADP+ + H2O
The 4 substrates of this enzyme are (S)-N-methylcoclaurine, NADPH, H+, and O2, whereas its 3 products are (S)-3'-hydroxy-N-methylcoclaurine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (3'-hydroxylating). This enzyme is also called N-methylcoclaurine 3'-hydroxylase and CYP80B1.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Orcinol%202-monooxygenase | In enzymology, an orcinol 2-monooxygenase () is an enzyme that catalyzes the chemical reaction
orcinol + NADH + H+ + O2 2,3,5-trihydroxytoluene + NAD+ + H2O
The 4 substrates of this enzyme are orcinol, NADH, H+, and O2, whereas its 3 products are 2,3,5-trihydroxytoluene, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is orcinol,NADH:oxygen oxidoreductase (2-hydroxylating). This enzyme is also called orcinol hydroxylase. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Peptide-aspartate%20beta-dioxygenase | In enzymology, a peptide-aspartate beta-dioxygenase (), a member of the alpha-ketoglutarate-dependent hydroxylases superfamily, is an enzyme that catalyzes the chemical reaction
peptide-L-aspartate + 2-oxoglutarate + O2 peptide-3-hydroxy-L-aspartate + succinate + CO2
The 3 substrates of this enzyme are peptide-L-aspartate, 2-oxoglutarate, and O2, whereas its 3 products are peptide-3-hydroxy-L-aspartate, succinate, and CO2.
It employs one cofactor, iron.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is peptide-L-aspartate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include aspartate beta-hydroxylase, and aspartylpeptide beta-dioxygenase.
References
Further reading section
Human 2OG oxygenases
EC 1.14.11
Iron enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Peptidylglycine%20monooxygenase | In enzymology, a peptidylglycine monooxygenase () is an enzyme that catalyzes the chemical reaction
peptidylglycine + ascorbate + O2 peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
The 3 substrates of this enzyme are peptidylglycine, ascorbate, and O2, whereas its 3 products are peptidyl(2-hydroxyglycine), dehydroascorbate, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is . Other names in common use include , , , , , , , , PAM-A, PAM-B, and PAM. It employs one cofactor, copper.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 1.14.17
Copper enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phenol%202-monooxygenase | In enzymology, a phenol 2-monooxygenase () is an enzyme that catalyzes the chemical reaction
phenol + NADPH + H+ + O2 catechol + NADP+ + H2O
The 4 substrates of this enzyme are phenol, NADPH, H+, and O2, whereas its 3 products are catechol, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is phenol,NADPH:oxygen oxidoreductase (2-hydroxylating). Other names in common use include phenol hydroxylase, and phenol o-hydroxylase. This enzyme participates in 3 metabolic pathways: gamma-hexachlorocyclohexane degradation, toluene and xylene degradation, and naphthalene and anthracene degradation. It employs one cofactor, FAD.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.14.13
NADPH-dependent enzymes
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phenylacetone%20monooxygenase | In enzymology, a phenylacetone monooxygenase () is an enzyme that catalyzes the chemical reaction
phenylacetone + NADPH + H+ + O2 benzyl acetate + NADP+ + H2O
The 4 substrates of this enzyme are phenylacetone, NADPH, H+, and O2, whereas its 3 products are benzyl acetate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is phenylacetone,NADPH:oxygen oxidoreductase. This enzyme is also called PAMO.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylcholine%2012-monooxygenase | In enzymology, a phosphatidylcholine 12-monooxygenase () is an enzyme that catalyzes the chemical reaction
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NADH + H+ + O2 1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + NAD+ + H2O
The 4 substrates of this enzyme are 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine, NADH, H+, and O2, whereas its 3 products are [[1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine]], NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine,NADH:oxygen oxidoreductase (12-hydroxylating). Other names in common use include ricinoleic acid synthase, oleate Delta12-hydroxylase, and oleate Delta12-monooxygenase.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phthalate%204%2C5-dioxygenase | In enzymology, a phthalate 4,5-dioxygenase () is an enzyme that catalyzes the chemical reaction
phthalate + NADH + H+ + O2 cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+
The 4 substrates of this enzyme are phthalate, NADH, H+, and O2, whereas its two products are cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor. The systematic name of this enzyme class is phthalate,NADH:oxygen oxidoreductase (4,5-hydroxylating). Other names in common use include PDO, and phthalate dioxygenase. This enzyme participates in 2,4-dichlorobenzoate degradation. It has 3 cofactors: iron, FMN, and Iron-sulfur.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Iron enzymes
Flavoproteins
Iron-sulfur enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phylloquinone%20monooxygenase%20%282%2C3-epoxidizing%29 | In enzymology, a phylloquinone monooxygenase (2,3-epoxidizing) () is an enzyme that catalyzes the chemical reaction
phylloquinone + AH2 + O2 2,3-epoxyphylloquinone + A + H2O
The three substrates of this enzyme are phylloquinone, an electron acceptor AH2, and O2, whereas its three products are 2,3-epoxyphylloquinone, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is . Other names in common use include , , , and .
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phytanoyl-CoA%20dioxygenase | In enzymology, a phytanoyl-CoA dioxygenase () is an enzyme that catalyzes the chemical reaction
phytanoyl-CoA + 2-oxoglutarate + O2 2-hydroxyphytanoyl-CoA + succinate + CO2
The three substrates of this enzyme are phytanoyl-CoA, 2-oxoglutarate (2OG), and O2, whereas its three products are 2-hydroxyphytanoyl-CoA, succinate, and CO2.
This enzyme belongs to the family of iron(II)-dependent oxygenases, which typically incorporate one atom of dioxygen into the substrate and one atom into the succinate carboxylate group. The mechanism is complex, but is believed to involve ordered binding of 2-oxoglutarate to the iron(II) containing enzyme followed by substrate. Binding of substrate causes displacement of a water molecule from the iron(II) cofactor, leaving a vacant coordination position to which dioxygen binds. A rearrangement occurs to form a high energy iron-oxygen species (which is generally thought to be an iron(IV)=O species) that performs the actual oxidation reaction.
Nomenclature
The systematic name of this enzyme class is phytanoyl-CoA, 2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating). This enzyme is also called phytanoyl-CoA hydroxylase and phytanoyl-CoA alpha-hydroxylase.
Examples
In humans, phytanoyl-CoA hydroxylase is encoded by the PHYH (aka PAHX) gene and is required for the alpha-oxidation of branched chain fatty acids (e.g. phytanic acid) in peroxisomes. PHYH deficiency results in the accumulation of large tissue stores of phytanic acid and is the major |
https://en.wikipedia.org/wiki/Plasmanylethanolamine%20desaturase | In enzymology, a plasmanylethanolamine desaturase () is an enzyme that catalyzes the chemical reaction
O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + AH2 + O2 O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + A + 2 H2O
The 3 substrates of this enzyme are O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine, an electron acceptor AH2, and O2, whereas its 3 products are O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine,hydrogen-donor:oxy gen oxidoreductase. Other names in common use include alkylacylglycerophosphoethanolamine desaturase, alkylacylglycero-phosphorylethanolamine dehydrogenase, dehydrogenase, alkyl-acylglycerophosphorylethanolamine, 1-O-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine desaturase, and 1-O-alkyl 2-acyl-sn-glycero-3-phosphorylethanolamine desaturase. This enzyme participates in ether lipid metabolism. It requires NADPH.
Plasmanylethanolamine desaturase used to be described as an orphan enzyme, that is one whose activity is known but whose identity (gene, protein sequence) is unknown. It has now been identified and corresponds to protein CarF in bacteria and TMEM189 in humans (and ani |
https://en.wikipedia.org/wiki/Precorrin-3B%20synthase | In enzymology, a precorrin-3B synthase () is an enzyme that catalyzes the chemical reaction
precorrin-3A + NADH + H+ + O2 precorrin-3B + NAD+ + H2O
The 4 substrates of this enzyme are precorrin 3A, NADH, H+, and O2, whereas its 3 products are precorrin 3B, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is precorrin-3A,NADH:oxygen oxidoreductase (20-hydroxylating). Other names in common use include precorrin-3X synthase, and CobG. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
Cobalamin biosynthesis
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Procollagen-proline%203-dioxygenase | In enzymology, a procollagen-proline 3-dioxygenase () is an enzyme that catalyzes the chemical reaction
procollagen L-proline + 2-oxoglutarate + O2 procollagen trans-3-hydroxy-L-proline + succinate + CO2
The enzyme is a member of the alpha-ketoglutarate-dependent hydroxylases superfamily. The 3 substrates of this enzyme are procollagen L-proline, 2-oxoglutarate, and O2, whereas its 3 products are procollagen trans-3-hydroxy-L-proline, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include proline,2-oxoglutarate 3-dioxygenase, prolyl 3-hydroxylase, protocollagen proline 3-hydroxylase, prolyl-4-hydroxyprolyl-glycyl-peptide, 2-oxoglutarate: oxygen, and oxidoreductase, 3-hydroxylating. It has 2 cofactors: iron, and Ascorbate.
References
Human 2OG oxygenases
EC 1.14.11
Iron enzymes
Ascorbate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Procollagen-proline%20dioxygenase | Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases. These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid, Fe2+, and ascorbate. This particular enzyme catalyzes the formation of (2S, 4R)-4-hydroxyproline, a compound that represents the most prevalent post-translational modification in the human proteome.
Enzyme mechanism
Procollagen-proline dioxygenase catalyzes the following reaction:
L-proline + alpha-ketoglutaric acid + O2 → (2S, 4R)-4-hydroxyproline + succinate + CO2
The mechanism for the reaction is similar to that of other dioxygenases, and occurs in two distinct stages: In the first, a highly reactive Fe(IV)=O species is produced. Molecular oxygen is bound end-on in an axial position, producing a dioxygen unit. Nucleophilic attack on C2 generates a tetrahedral intermediate, with loss of the double bond in the dioxygen unit and bonds to iron and the alpha carbon of 2-oxoglutarate. Subsequent elimination of CO2 coincides with the formation of the Fe(IV)=O species. The second stage involves the abstraction of the pro-R hydrogen atom from C-4 of the proline substrate followed by radical combination, which yields hydroxyproline.
As a consequence of the reaction mechanism, one molecule of 2-oxoglutarate is decarboxylated, forming succinate. This succinate is hydrolyzed and replaced with |
https://en.wikipedia.org/wiki/Progesterone%2011alpha-monooxygenase | In enzymology, a progesterone 11alpha-monooxygenase () is an enzyme that catalyzes the chemical reaction
progesterone + AH2 + O2 11alpha-hydroxyprogesterone + A + H2O
The 3 substrates of this enzyme are progesterone, AH2, and O2, whereas its 3 products are 11alpha-hydroxyprogesterone, A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is {{chem name|progesterone,hydrogen-donor:oxygen oxidoreductase (11alpha-hydroxylating)}}. This enzyme is also called . This enzyme participates in c21-steroid hormone metabolism.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Progesterone%20monooxygenase | In enzymology, a progesterone monooxygenase () is an enzyme that catalyzes the chemical reaction
progesterone + AH2 + O2 testosterone acetate + A + H2O
The 3 substrates of this enzyme are progesterone, AH2, and O2, whereas its 3 products are testosterone acetate, A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O miscellaneous. The systematic name of this enzyme class is . This enzyme is also called progesterone hydroxylase.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Proline%203-hydroxylase | In enzymology, a proline 3-hydroxylase () is an enzyme that catalyzes the chemical reaction
L-proline + 2-oxoglutarate + O2 cis-3-hydroxy-L-proline + succinate + CO2
The 3 substrates of this enzyme are L-proline, 2-oxoglutarate, and O2, whereas its 3 products are cis-3-hydroxy-L-proline, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). This enzyme is also called P-3-H.
References
EC 1.14.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Protopine%206-monooxygenase | In enzymology, a protopine 6-monooxygenase () is an enzyme that catalyzes the chemical reaction
protopine + NADPH + H+ + O2 6-hydroxyprotopine + NADP+ + H2O
The 4 substrates of this enzyme are protopine, NADPH, H+, and O2, whereas its 3 products are 6-hydroxyprotopine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is protopine,NADPH:oxygen oxidoreductase (6-hydroxylating). This enzyme is also called protopine 6-hydroxylase. This enzyme participates in alkaloid biosynthesis i.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Psoralen%20synthase | In enzymology, a psoralen synthase () is an enzyme that catalyzes the chemical reaction
(+)-marmesin + NADPH + H+ + O2 psoralen + NADP+ + acetone + 2 H2O
The 4 substrates of this enzyme are (+)-marmesin, NADPH, H+, and O2, whereas its 4 products are psoralen, NADP+, acetone, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (?). This enzyme is also called CYP71AJ1.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyrimidine-deoxynucleoside%201%27-dioxygenase | In enzymology, a pyrimidine-deoxynucleoside 1'-dioxygenase () is an enzyme that catalyzes the chemical reaction
2'-deoxyuridine + 2-oxoglutarate + O2 uracil + 2-deoxyribonolactone + succinate + CO2
The 3 substrates of this enzyme are 2'-deoxyuridine, 2-oxoglutarate, and O2, whereas its 4 products are uracil, 2-deoxyribonolactone, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is 2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (1'-hydroxylating). This enzyme is also called deoxyuridine-uridine 1'-dioxygenase. It has 2 cofactors: iron, and Ascorbate.
References
EC 1.14.11
Iron enzymes
Ascorbate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyrimidine-deoxynucleoside%202%27-dioxygenase | In enzymology, a pyrimidine-deoxynucleoside 2'-dioxygenase () is an enzyme that catalyzes the chemical reaction
2'-deoxyuridine + 2-oxoglutarate + O2 uridine + succinate + CO2
The 3 substrates of this enzyme are 2'-deoxyuridine, 2-oxoglutarate, and O2, whereas its 3 products are uridine, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is 2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (2'-hydroxylating). Other names in common use include deoxyuridine 2'-dioxygenase, deoxyuridine 2'-hydroxylase, pyrimidine deoxyribonucleoside 2'-hydroxylase, thymidine 2'-dioxygenase, thymidine 2'-hydroxylase, thymidine 2-oxoglutarate dioxygenase, and thymidine dioxygenase. It has 2 cofactors: iron, and Ascorbate.
References
EC 1.14.11
Iron enzymes
Ascorbate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Questin%20monooxygenase | In enzymology, a questin monooxygenase () is an enzyme that catalyzes the chemical reaction
questin + NADPH + H+ + O2 demethylsulochrin + NADP+ + H2O
The 4 substrates of this enzyme are questin, NADPH, H+, and O2, whereas its 3 products are demethylsulochrin, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is questin,NADPH:oxygen oxidoreductase (hydroxylating, anthraquinone-ring-opening). This enzyme is also called questin oxygenase.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Quinine%203-monooxygenase | In enzymology, a quinine 3-monooxygenase () is an enzyme that catalyzes the chemical reaction
quinine + NADPH + H+ + O2 3-hydroxyquinine + NADP+ + H2O
The 4 substrates of this enzyme are quinine, NADPH, H+, and O2, whereas its 3 products are 3-hydroxyquinine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is quinine,NADPH:oxygen oxidoreductase. This enzyme is also called quinine 3-hydroxylase.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28R%29-limonene%206-monooxygenase | In enzymology, a (R)-limonene 6-monooxygenase () is an enzyme that catalyzes the chemical reaction
(+)-(R)-limonene + NADPH + H + O (+)-trans-carveol + NADP + HO
The 4 substrates of this enzyme are (+)-(R)-limonene, NADPH, H, and O, whereas its 3 products are (+)-trans-carveol, NADP, and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (R)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating). Other names in common use include (+)-limonene-6-hydroxylase, and (+)-limonene 6-monooxygenase. This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation.
See also
CYP2C19
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Salicylate%201-monooxygenase | Salicylate 1-Monooxygenase: Enzyme Involved in Aromatic Compound Degradation
Introduction:
Salicylate 1-monooxygenase is an enzyme that plays a crucial role in the degradation of salicylate and aromatic compounds in microbial metabolism. It belongs to the family of oxidoreductases and is classified under the EC number 1.14.13.1. In this article, we will explore the enzyme's reaction pathway, its presence in different organisms, its cellular function, known crystal structures, active sites, and the connection between structure and function.
EC Number: 1.14.13.1 - Understanding its Significance
The EC number of an enzyme provides a systematic classification based on the type of reaction it catalyzes. For salicylate 1-monooxygenase, the EC number 1.14.13.1 signifies that this enzyme is an oxidoreductase (1) that utilizes molecular oxygen (O2) as the electron acceptor and acts on paired donors (D) with O2 as the oxidant (14).
Reaction Pathway of Salicylate 1-Monooxygenase:
The primary function of salicylate 1-monooxygenase is to catalyze the conversion of salicylate to catechol in the presence of NADH, H+, and O2. The reaction can be represented as follows:
Salicylate + NADH + H+ + O2 → Catechol + NAD+ + H2O
The enzyme carries out hydroxylation at the aromatic ring of salicylate, resulting in the formation of catechol. This process involves the transfer of an oxygen atom from molecular oxygen to salicylate, leading to the formation of a hydroxyl group on the aromatic ring |
https://en.wikipedia.org/wiki/Salutaridine%20synthase | In enzymology, a salutaridine synthase () is an enzyme that catalyzes the chemical reaction
(R)-reticuline + NADPH + H+ + O2 salutaridine + NADP+ + 2 H2O
The 4 substrates of this enzyme are (R)-reticuline, NADPH, H+, and O2, whereas its 3 products are salutaridine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and the other dehydrogenated. The systematic name of this enzyme class is (R)-reticuline,NADPH:oxygen oxidoreductase (C-C phenol-coupling). This enzyme is also called (R)-reticuline oxidase (C-C phenol-coupling). This enzyme participates in alkaloid biosynthesis i.
References
EC 1.14.21
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-canadine%20synthase | In enzymology, a (S)-canadine synthase () is an enzyme that catalyzes the chemical reaction
(S)-tetrahydrocolumbamine + NADPH + H + O (S)-canadine + NADP + 2 HO
The 4 substrates of this enzyme are (S)-tetrahydrocolumbamine, NADPH, H, and O, whereas its 3 products are Canadine, NADP, and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O with NADH or NADPH as one donor, and the other dehydrogenated. The systematic name of this enzyme class is (S)-tetrahydrocolumbamine,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming). Other names in common use include (S)-tetrahydroberberine synthase, and (S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming). This enzyme participates in alkaloid biosynthesis i. It employs one cofactor, heme-thiolate(P-450).
References
EC 1.14.21
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-cheilanthifoline%20synthase | In enzymology, a (S)-cheilanthifoline synthase () is an enzyme that catalyzes the chemical reaction
(S)-scoulerine + NADPH + H + O (S)-cheilanthifoline + NADP + 2 HO
The 4 substrates of this enzyme are (S)-scoulerine, NADPH, H, and O, whereas its 3 products are (S)-cheilanthifoline, NADP, and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and the other dehydrogenated. The systematic name of this enzyme class is (S)-scoulerine,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming). This enzyme is also called (S)-scoulerine oxidase (methylenedioxy-bridge-forming). This enzyme participates in alkaloid biosynthesis i.
References
EC 1.14.21
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Senecionine%20N-oxygenase | In enzymology, a senecionine N-oxygenase () is an enzyme that catalyzes the chemical reaction
senecionine + NADPH + H+ + O2 senecionine N-oxide + NADP+ + H2O
The 4 substrates of this enzyme are senecionine, NADPH, H+, and O2, whereas its 3 products are senecionine N-oxide, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is senecionine,NADPH:oxygen oxidoreductase (N-oxide-forming). Other names in common use include senecionine monooxygenase (N-oxide-forming) and SNO.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-limonene%203-monooxygenase | In enzymology, a (S)-limonene 3-monooxygenase () is an enzyme that catalyzes the chemical reaction
(-)-(S)-limonene + NADPH + H + O (-)-trans-isopiperitenol + NADP + HO
The 4 substrates of this enzyme are (-)-(S)-limonene, NADPH, H, and O, whereas its 3 products are (-)-trans-isopiperitenol, NADP, and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (S)-limonene,NADPH:oxygen oxidoreductase (3-hydroxylating). Other names in common use include (-)-limonene 3-hydroxylase, (-)-limonene 3-monooxygenase, and (-)-limonene,NADPH:oxygen oxidoreductase (3-hydroxylating). This enzyme participates in monoterpenoid biosynthesis. It employs one cofactor, heme.
References
EC 1.14.13
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-limonene%206-monooxygenase | In enzymology, a (S)-limonene 6-monooxygenase () is an enzyme that catalyzes the chemical reaction
(-)-(S)-limonene + NADPH + H + O (-)-trans-carveol + NADP + HO
The 4 substrates of this enzyme are (-)-(S)-limonene, NADPH, H, and O, whereas its 3 products are (-)-trans-carveol, NADP, and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (S)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating). Other names in common use include (-)-limonene 6-hydroxylase, (-)-limonene 6-monooxygenase, and (-)-limonene,NADPH:oxygen oxidoreductase (6-hydroxylating). This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation. It employs one cofactor, heme.
See also
CYP2C19
References
EC 1.14.13
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-limonene%207-monooxygenase | In enzymology, a (S)-limonene 7-monooxygenase () is an enzyme that catalyzes the chemical reaction
(-)-(S)-limonene + NADPH + H + O (-)-perillyl alcohol + NADP + HO
The 4 substrates of this enzyme are (-)-(S)-limonene, NADPH, H, and O, whereas its 3 products are (-)-perillyl alcohol, NADP, and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (S)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating). Other names in common use include (-)-limonene 7-monooxygenase, (-)-limonene hydroxylase, (-)-limonene monooxygenase, and (-)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating). This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation. It employs one cofactor, heme.
References
EC 1.14.13
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-stylopine%20synthase | In enzymology, a (S)-stylopine synthase () is an enzyme that catalyzes the chemical reaction
(S)-cheilanthifoline + NADPH + H + O (S)-stylopine + NADP + 2 HO
The 4 substrates of this enzyme are (S)-cheilanthifoline, NADPH, H, and O, whereas its 3 products are (S)-stylopine, NADP, and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and the other dehydrogenated. The systematic name of this enzyme class is (S)-cheilanthifoline,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming). This enzyme is also called (S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming). This enzyme participates in alkaloid biosynthesis.
References
EC 1.14.21
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Stearoyl-CoA%209-desaturase | Stearoyl-CoA desaturase (Δ-9-desaturase) is an endoplasmic reticulum enzyme that catalyzes the rate-limiting step in the formation of monounsaturated fatty acids (MUFAs), specifically oleate and palmitoleate from stearoyl-CoA and palmitoyl-CoA. Oleate and palmitoleate are major components of membrane phospholipids, cholesterol esters and alkyl-diacylglycerol. In humans, the enzyme is encoded by the SCD gene.
Stearoyl-CoA desaturase-1 is a key enzyme in fatty acid metabolism. It is responsible for forming a double bond in stearoyl-CoA. This is how the monounsaturated fatty acid oleic acid is produced from the saturated fatty acid, stearic acid.
A series of redox reactions, during which two electrons flow from NADH to flavoprotein cytochrome b5, then to the electron acceptor cytochrome b5 as well as molecular oxygen introduces a single double bond within a row of methylene fatty acyl-CoA substrates. The complexed enzyme adds a single double bond between the C9 and C10 of long-chain acyl-CoAs from de-novo synthesis.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with oxidation of a pair of donors resulting in the reduction of O to two molecules of water. The systematic name of this enzyme class is stearoyl-CoA,ferrocytochrome-b5:oxygen oxidoreductase (9,10-dehydrogenating). Other names in common use include Delta |
https://en.wikipedia.org/wiki/Steroid%2011beta-monooxygenase | In enzymology, a steroid 11beta-monooxygenase () is an enzyme that catalyzes the chemical reaction
a steroid + reduced adrenal ferredoxin + O2 an 11beta-hydroxysteroid + oxidized adrenal ferredoxin + H2O
The 3 substrates of this enzyme are steroid, reduced adrenal ferredoxin, and O2, whereas its 3 products are 11beta-hydroxysteroid, oxidized adrenal ferredoxin, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation o one atom of oxygen into the other donor. The systematic name of this enzyme class is steroid,reduced-adrenal-ferredoxin:oxygen oxidoreductase (11beta-hydroxylating). Other names in common use include steroid 11beta-hydroxylase, steroid 11beta/18-hydroxylase, and oxygenase, steroid 11beta -mono-. This enzyme participates in c21-steroid hormone metabolism and androgen and estrogen metabolism. It employs one cofactor, heme.
References
EC 1.14.15
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Steroid%2017alpha-monooxygenase | In enzymology, a steroid 17alpha-monooxygenase () is an enzyme that catalyzes the chemical reaction
a steroid + AH2 + O2 a 17alpha-hydroxysteroid + A + H2O
The 3 substrates of this enzyme are steroid, an electron acceptor AH2, and O2, whereas its 3 products are 17alpha-hydroxysteroid, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is steroid,hydrogen-donor:oxygen oxidoreductase (17alpha-hydroxylating). Other names in common use include steroid 17alpha-hydroxylase, cytochrome P-45017alpha, cytochrome P-450 (P-45017alpha,lyase), and 17alpha-hydroxylase-C17,20 lyase. This enzyme participates in c21-steroid hormone metabolism. It has 3 cofactors: NADH, NADPH, and Heme.
References
External links
EC 1.14.99
NADH-dependent enzymes
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Steroid%209alpha-monooxygenase | In enzymology, a steroid 9alpha-monooxygenase () is an enzyme that catalyzes the chemical reaction
pregna-4,9(11)-diene-3,20-dione + AH2 + O2 9,11alpha-epoxypregn-4-ene-3,20-dione + A + H2O
The 3 substrates of this enzyme are pregna-4,9(11)-diene-3,20-dione, an electron acceptor AH2, and O2, whereas its 3 products are 9,11alpha-epoxypregn-4-ene-3,20-dione, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is steroid,hydrogen-donor:oxygen oxidoreductase (9-epoxidizing). This enzyme is also called steroid 9alpha-hydroxylase. It has 2 cofactors: FMN, and Iron-sulfur.
References
EC 1.14.99
Flavoproteins
Iron-sulfur enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sterol%2014-demethylase | In enzymology, a sterol 14-demethylase () is an enzyme of the Cytochrome P450 (CYP) superfamily. It is any member of the CYP51 family. It catalyzes a chemical reaction such as:
obtusifoliol + 3 O2 + 3 NADPH + 3 H+ 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 3 NADP+ + 4 H2O
The 4 substrates here are obtusifoliol, O2, NADPH, and H+, whereas its 4 products are 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol, formate, NADP+, and H2O.
Although the lanosterol 14α-demethylase is present in a wide variety of organisms, the enzyme is studied primarily in the context of fungi, where it plays an essential role in mediating membrane permeability. In fungi, CYP51 catalyzes the demethylation of lanosterol to create an important precursor that is eventually converted into ergosterol. This steroid then makes its way throughout the cell, where it alters the permeability and rigidity of plasma membranes much as cholesterol does in animals. Because ergosterol constitutes a fundamental component of fungal membranes, many antifungal medications have been developed to inhibit 14α-demethylase activity and prevent the production of this key compound.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor |
https://en.wikipedia.org/wiki/Tabersonine%2016-hydroxylase | In enzymology, a tabersonine 16-hydroxylase () is an enzyme that catalyzes the chemical reaction
tabersonine + NADPH + H+ + O2 16-hydroxytabersonine + NADP+ + H2O
The 4 substrates of this enzyme are tabersonine, NADPH, H+, and O2, whereas its 3 products are 16-hydroxytabersonine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is tabersonine,NADPH:oxygen oxidoreductase (16-hydroxylating). Other names in common use include tabersonine-11-hydroxylase, and T11H. This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Taurine%20dioxygenase | In enzymology, a taurine dioxygenase () is an enzyme that catalyzes the chemical reaction.
taurine + 2-oxoglutarate + O2 sulfite + aminoacetaldehyde + succinate + CO2
The 3 substrates of this enzyme are taurine, 2-oxoglutarate, and O2, whereas its 4 products are sulfite, aminoacetaldehyde, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is taurine, 2-oxoglutarate:O2 oxidoreductase (sulfite-forming). Other names in common use include 2-aminoethanesulfonate dioxygenase, and alpha-ketoglutarate-dependent taurine dioxygenase. This enzyme participates in taurine and hypotaurine metabolism. It has 3 cofactors: iron, Ascorbate, and Fe2+.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
Mechanism
Initiating steps
In the decomposition of taurine, it has been shown that molecular oxygen is activated by Iron II, which lies in the coordinating complex of taurine dioxygenase. Here the enzyme with conjunction of an Iron II and 2-oxoglutarate maintain non-covalent bonds by electrostatic interactions, and coordinate a nucleophilic attack from dioxygen on 2-oxoglutarate carbon number 2. This |
https://en.wikipedia.org/wiki/Taxadiene%205alpha-hydroxylase | In enzymology, a taxadiene 5alpha-hydroxylase () is an enzyme that catalyzes the chemical reaction
taxa-4,11-diene + AH2 + O2 taxa-4(20),11-dien-5alpha-ol + A + H2O
The 3 substrates of this enzyme are taxa-4,11-diene, an electron acceptor AH2, and O2, whereas its 3 products are taxa-4(20),11-dien-5alpha-ol, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is taxa-4,11-diene,hydrogen-donor:oxygen oxidoreductase (5alpha-hydroxylating). This enzyme participates in diterpenoid biosynthesis.
References
Further reading
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Taxane%2010beta-hydroxylase | In enzymology, a taxane 10beta-hydroxylase () is an enzyme that catalyzes the chemical reaction
taxa-4(20),11-dien-5alpha-yl acetate + NADPH + H+ + O2 10beta-hydroxytaxa-4(20),11-dien-5alpha-yl acetate + NADP+ + H2O
The 4 substrates of this enzyme are taxa-4(20),11-dien-5alpha-yl acetate, NADPH, H+, and O2, whereas its 3 products are 10beta-hydroxytaxa-4(20),11-dien-5alpha-yl acetate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is taxa-4(20),11-dien-5alpha-yl acetate,NADPH:oxygen oxidoreductase (10beta-hydroxylating). This enzyme participates in diterpenoid biosynthesis.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Taxane%2013alpha-hydroxylase | In enzymology, a taxane 13alpha-hydroxylase () is an enzyme that catalyzes the chemical reaction
taxa-4(20),11-dien-5alpha-ol + NADPH + H+ + O2 taxa-4(20),11-dien-5alpha,13alpha-diol + NADP+ + H2O
The 4 substrates of this enzyme are taxa-4(20),11-dien-5alpha-ol, NADPH, H+, and O2, whereas its 3 products are taxa-4(20),11-dien-5alpha,13alpha-diol, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is taxa-4(20),11-dien-5alpha-ol,NADPH:oxygen oxidoreductase (13alpha-hydroxylating). This enzyme participates in diterpenoid biosynthesis.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Taxifolin%208-monooxygenase | In enzymology, a taxifolin 8-monooxygenase () is an enzyme that catalyzes the chemical reaction
taxifolin + NAD(P)H + H+ + O2 2,3-dihydrogossypetin + NAD(P)+ + H2O
The 5 substrates of this enzyme are taxifolin, NADH, NADPH, H+, and O2, whereas its 4 products are 2,3-dihydrogossypetin, NAD+, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is taxifolin,NAD(P)H:oxygen oxidoreductase (8-hydroxylating). This enzyme is also called taxifolin hydroxylase. It has 2 cofactors: FAD, and Flavoprotein.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Terephthalate%201%2C2-dioxygenase | In enzymology, a terephthalate 1,2-dioxygenase () is an enzyme that catalyzes the chemical reaction
terephthalate + NADH + H+ + O2 (1R,6S)-dihydroxycyclohexa-2,4-diene-1,4-dicarboxylate + NAD+
The 4 substrates of this enzyme are terephthalate, NADH, H+, and O2, whereas its two products are (1R,6S)-dihydroxycyclohexa-2,4-diene-1,4-dicarboxylate and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is benzene-1,4-dicarboxylate,NADH:oxygen oxidoreductase (1,2-hydroxylating). Other names in common use include benzene-1,4-dicarboxylate 1,2-dioxygenase, and 1,4-dicarboxybenzoate 1,2-dioxygenase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiophene-2-carbonyl-CoA%20monooxygenase | In enzymology, a thiophene-2-carbonyl-CoA monooxygenase () is an enzyme that catalyzes the chemical reaction
thiophene-2-carbonyl-CoA + AH2 + O2 5-hydroxythiophene-2-carbonyl-CoA + A + H2O
The three substrates of this enzyme are thiophene-2-carbonyl-CoA, an electron acceptor AH2, and O2. Its three products are 5-hydroxythiophene-2-carbonyl-CoA, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O miscellaneous. The systematic name of this enzyme class is thiophene-2-carbonyl-CoA, hydrogen-donor:oxygen oxidoreductase. Other names in common use include thiophene-2-carboxyl-CoA dehydrogenase, thiophene-2-carboxyl-CoA hydroxylase, and thiophene-2-carboxyl-CoA monooxygenase.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thymine%20dioxygenase | In enzymology, a thymine dioxygenase () is an enzyme that catalyzes the chemical reaction
thymine + 2-oxoglutarate + O2 5-hydroxymethyluracil + succinate + CO2
The 3 substrates of this enzyme are thymine, 2-oxoglutarate, and O2, whereas its 3 products are 5-hydroxymethyluracil, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is thymine,2-oxoglutarate:oxygen oxidoreductase (7-hydroxylating). Other names in common use include thymine 7-hydroxylase, 5-hydroxy-methyluracil dioxygenase, and 5-hydroxymethyluracil oxygenase. It has 2 cofactors: iron, and Ascorbate.
References
EC 1.14.11
Iron enzymes
Ascorbate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Toluene%20dioxygenase | In enzymology, a toluene dioxygenase () is an enzyme that catalyzes the chemical reaction
toluene + NADH + H+ + O2 (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
The 4 substrates of this enzyme are toluene, NADH, H+, and O2, whereas its two products are (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is toluene,NADH:oxygen oxidoreductase (1,2-hydroxylating). This enzyme is also called toluene 2,3-dioxygenase. This enzyme participates in toluene and xylene degradation.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trans-cinnamate%202-monooxygenase | In enzymology, a trans-cinnamate 2-monooxygenase () is an enzyme that catalyzes the chemical reaction
trans-cinnamate + NADPH + H+ + O2 2-hydroxycinnamate + NADP+ + H2O
The 4 substrates of this enzyme are trans-cinnamate, NADPH, H+, and O2, whereas its 3 products are 2-hydroxycinnamate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is trans-cinnamate,NADPH:oxygen oxidoreductase (2-hydroxylating). Other names in common use include cinnamic acid 2-hydroxylase, cinnamate 2-monooxygenase, cinnamic 2-hydroxylase, cinnamate 2-hydroxylase, and trans-cinnamic acid 2-hydroxylase. This enzyme participates in phenylalanine metabolism and phenylpropanoid biosynthesis.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/Trans-cinnamate%204-monooxygenase | In enzymology, a trans-cinnamate 4-monooxygenase () is an enzyme that catalyzes the chemical reaction
trans-cinnamate + NADPH + H+ + O2 4-hydroxycinnamate + NADP+ + H2O
The 4 substrates of this enzyme are trans-cinnamate, NADPH, H+, and O2, whereas its 3 products are 4-hydroxycinnamate, NADP+, and H2O. This enzyme participates in phenylalanine metabolism and phenylpropanoid biosynthesis. It employs one cofactor, heme.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor.
Nomenclature
The systematic name of this enzyme class is trans-cinnamate,NADPH:oxygen oxidoreductase (4-hydroxylating). Other names in common use include:
cinnamic acid 4-hydroxylase,
oxygenase, cinnamate 4-mono-,
CA4H (gene name),
CYP73A1 (gene name),
cytochrome P450 cinnamate 4-hydroxylase,
cinnamate 4-hydroxylase,
cinnamate 4-monooxygenase,
cinnamate hydroxylase,
cinnamic 4-hydroxylase,
cinnamic acid 4-monooxygenase,
cinnamic acid p-hydroxylase,
hydroxylase, cinnamate 4-,
t-cinnamic acid hydroxylase,
trans-cinnamate 4-hydroxylase, and
trans-cinnamic acid 4-hydroxylase.
References
Further reading
EC 1.14.13
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trimethyllysine%20dioxygenase | In enzymology, a trimethyllysine dioxygenase (TMLH; ) is an enzyme that catalyzes the chemical reaction
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
TMLH is a member of the alpha-ketoglutarate-dependent hydroxylases superfamily. The 3 substrates of this enzyme are N6,N6,N6-trimethyl-L-lysine, 2-oxoglutarate, and O2, whereas its 3 products are 3-hydroxy-N6,N6,N6-trimethyl-L-lysine, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is N6,N6,N6-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include trimethyllysine alpha-ketoglutarate dioxygenase, TML-alpha-ketoglutarate dioxygenase, TML hydroxylase, 6-N,6-N,6-N-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase, and (3-hydroxylating). This enzyme participates in lysine degradation and L-carnitine biosynthesis and requires the presence of iron and ascorbate.
See also
Carnitine biosynthesis
γ-Butyrobetaine hydroxylase
4-N-Trimethylaminobutyraldehyde dehydrogenase
References
Human 2OG oxygenases
EC 1.14.11
Iron enzymes
Ascorbate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Unspecific%20monooxygenase | In enzymology, an unspecific monooxygenase () is an enzyme that catalyzes the chemical reaction
RH + reduced flavoprotein + O2 ROH + oxidized flavoprotein + H2O
The 3 substrates of this enzyme are RH (reduced substrate), reduced flavoprotein, and O2, whereas its 3 products are ROH (oxidized substrate), oxidized flavoprotein, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is . Other names in common use include microsomal monooxygenase, xenobiotic monooxygenase, aryl-4-monooxygenase, aryl hydrocarbon hydroxylase, microsomal P-450, flavoprotein-linked monooxygenase, and flavoprotein monooxygenase. This enzyme participates in 7 metabolic pathways: fatty acid metabolism, androgen and estrogen metabolism, gamma-hexachlorocyclohexane degradation, tryptophan metabolism, arachidonic acid metabolism, linoleic acid metabolism, and metabolism of xenobiotics by cytochrome p450. It employs one cofactor, heme.
Structural studies
As of late 2007, 53 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
References
|
https://en.wikipedia.org/wiki/Vanillate%20monooxygenase | In enzymology, a vanillate monooxygenase () is an enzyme that catalyzes the chemical reaction
+ O2 + NADH + H+ + NAD+ + H2O + formaldehyde
The 4 substrates of this enzyme are vanillate, O2, NADH, and H+, whereas its 4 products are 3,4-dihydroxybenzoate, NAD+, H2O, and formaldehyde.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is vanillate:oxygen oxidoreductase (demethylating). Other names in common use include 4-hydroxy-3-methoxybenzoate demethylase, and vanillate demethylase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vinorine%20hydroxylase | In enzymology, a vinorine hydroxylase (, Formerly ) is an enzyme that catalyzes the chemical reaction
vinorine + NADPH + H+ + O2 vomilenine + NADP+ + H2O
The 4 substrates of this enzyme are vinorine, NADPH, H+, and O2, whereas its 3 products are vomilenine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is vinorine,NADPH:oxygen oxidoreductase (21alpha-hydroxylating). This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 1.14.14
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Port%20%28medical%29 | In medicine, a port is a small medical appliance that is installed beneath the skin. A catheter (plastic tube) connects the port to a vein. Under the skin, the port has a septum (a silicone membrane) through which drugs can be injected and blood samples can be drawn many times, usually with less discomfort for the patient (and clinician) than a more typical "needle stick".
Terminology
A port is more correctly known as a "totally implantable venous access device". They are also commonly referred to as a Portacath or Chemo port. Brand names include Eco Port, Clip-a-Port, SmartPort, Microport, Bardport, PowerPort, Passport, Port-a-Cath, Infuse-a-Port, Medi-Port, and Bioflo.
Structure
Ports are used mostly to treat hematology and oncology patients. Ports were previously adapted for use in hemodialysis patients, but were found to be associated with increased rate of infections and are no longer available in the US.
The port is usually inserted in the upper chest (known as a "chest port"), just below the clavicle or collar bone, with the catheter inserted into the jugular vein.
A port consists of a reservoir compartment (the portal) that has a silicone bubble for needle insertion (the septum), with an attached plastic tube (the catheter). The device is surgically inserted under the skin in the upper chest or in the arm and appears as a bump under the skin. It requires no special maintenance other than occasional flushing to keep clear. It is completely internal so swimming |
https://en.wikipedia.org/wiki/Gibson%20v.%20United%20States | Gibson v. United States, 329 U.S. 338 (1946), was a case in which the Supreme Court of the United States ruled that a Jehovah's Witness minister could appeal his classification without first appearing at induction camp.
References
External links
1946 in United States case law
United States Supreme Court cases
United States Supreme Court cases of the Vinson Court
Jehovah's Witnesses litigation in the United States
1946 in religion
Christianity and law in the 20th century |
https://en.wikipedia.org/wiki/Brainbow | Brainbow is a process by which individual neurons in the brain can be distinguished from neighboring neurons using fluorescent proteins. By randomly expressing different ratios of red, green, and blue derivatives of green fluorescent protein in individual neurons, it is possible to flag each neuron with a distinctive color. This process has been a major contribution to the field of neural connectomics.
The technique was originally developed in 2007 by a team led by Jeff W. Lichtman and Joshua R. Sanes, both at Harvard University. The original technique has recently been adapted for use with other model research organisms including the fruit fly (Drosophila melanogaster), zebrafish (Danio rerio), and Arabidopsis thaliana.
While earlier labeling techniques allowed for the mapping of only a few neurons, this new method allows more than 100 differently mapped neurons to be simultaneously and differentially illuminated in this manner. This leads to its characteristic multicolored appearance on imaging, earning its name and winning awards in science photography competitions.
History and development
Brainbow was initially developed by Jeff W. Lichtman and Joshua R. Sanes at Washington University in St. Louis, though they have moved to Harvard University since then. The team constructed Brainbow using a two-step process: first, a specific genetic construct was generated that could be recombined in multiple arrangements to produce one of either three or four colors based on the p |
https://en.wikipedia.org/wiki/Takashi%20Gojobori | is a Japanese molecular biologist, Vice-Director of the National Institute of Genetics (NIG) and the DNA Data Bank of Japan (DDBJ) at NIG, in Mishima, Japan. Gojobori is a Distinguished Professor at King Abdullah University of Science and Technology (KAUST) in Thuwal, Saudi Arabia. He is a Professor of Bioscience and Acting Director at the Computational Bioscience Research Center at KAUST.
He has also been co-appointed as the Special Research Consultant of the National Institute of Advanced Industrial Science and Technology (AIST), and acts as a visiting professor of Keio University, University of Tokyo, and Tokyo Institute of Technology.
He is an Associate Member of the European Molecular Biology Organization (EMBO), a Member of Academia Europea and an Academician Member of the Pontifical Academy of Sciences, Vatican.
Education
Gojobori finished his Ph.D. in Theoretical Population Genetics (1979) at Kyushu University, Japan. He was a research associate and research assistant professor at the University of Texas Health Science Center at Houston (UTHealth) for 4 years (1979–1983). He was also visiting assistant professor at Washington University in St. Louis (1985, 1986) and visiting research fellow at the Imperial Cancer Research Fund (ICRF) in London (1989).
Research
He is the Founding Editor of the journal Genome Biology and Evolution, the Executive Editor of the journal Gene, Academic Editor of FEBS Letters, Associate Editor of Molecular Biology and Evolution and PLO |
https://en.wikipedia.org/wiki/Marius%20Matei | Marius Matei (born 1 February 1984) is a Romanian footballer who plays as a forward for Avântul Valea Mărului.
Statistics
Career honours
FC Vaslui
UEFA Intertoto Cup
Winner: 2008
References
External links
1984 births
Living people
Romanian men's footballers
Men's association football forwards
Liga I players
Liga II players
AFC Dacia Unirea Brăila players
CS Sporting Vaslui players
ASC Oțelul Galați players
FC Botoșani players
FCV Farul Constanța players
FC Voluntari players
FC Brașov (1936) players
ACS Foresta Suceava players
CS Luceafărul Oradea players
Footballers from Galați |
https://en.wikipedia.org/wiki/MMP3 | Stromelysin-1 also known as matrix metalloproteinase-3 (MMP-3) is an enzyme that in humans is encoded by the MMP3 gene. The MMP3 gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP-3 has an estimated molecular weight of 54 kDa.
Function
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix proteins and during tissue remodeling in normal physiological processes, such as embryonic development and reproduction, as well as in disease processes, such as arthritis, and tumour metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases.
The MMP-3 enzyme degrades collagen types II, III, IV, IX, and X, proteoglycans, fibronectin, laminin, and elastin. In addition, MMP-3 can also activate other MMPs such as MMP-1, MMP-7, and MMP-9, rendering MMP-3 crucial in connective tissue remodeling. The enzyme is also thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation.
In addition to classical roles for MMP3 in extracellular space, MMP3 can enter in cellular nuclei and control transcription.
Gene regulation
MMP3 itself can enter in nuclei of cells and regulate target gene such as CTGF/CCN2 gene.
Expression of MMP3 is primarily regulated at the level of transcription, where the promoter of the gene responds to various stimuli, including growth factors, cytokines, tumor promoters, and oncogene products. A p |
https://en.wikipedia.org/wiki/Picenadol | Picenadol (LY-97435) is a 4-phenylpiperidine derivative that is an opioid analgesic drug developed by Eli Lilly in the 1970s.
Picenadol is an effective analgesic with similar efficacy to pethidine (meperidine). It has been investigated for some applications such as obstetrics and dentistry, but never commercialised.
It is unusual in that one enantiomer is a pure μ-opioid agonist, while the other is an antagonist. The (3R,4R) isomer is the agonist, while (3S,4S) is antagonist. This means that the racemic mix of the two enantiomers is a mixed agonist-antagonist, with relatively low abuse potential, and little of the κ-opioid activity that tends to cause problems with other opioid mixed agonist-antagonists such as pentazocine.
Synthesis
See also
Ketobemidone
References
Synthetic opioids
4-Phenylpiperidines
Phenols
Mu-opioid receptor agonists |
https://en.wikipedia.org/wiki/Neuropeptide%20S%20receptor | The neuropeptide S receptor (NPSR) is a member of the G-protein coupled receptor superfamily of integral membrane proteins which binds neuropeptide S (NPS). It was formerly an orphan receptor, GPR154, until the discovery of neuropeptide S as the endogenous ligand. Increased expression of this gene in ciliated cells of the respiratory epithelium and in bronchial smooth muscle cells is associated with asthma. This gene is a member of the G protein-coupled receptor 1 family and encodes a plasma membrane protein. Mutations in this gene have also been associated with this disease.
Clinical significance
In the CNS, activation of the NPSR by NPS promotes arousal and anxiolytic-like effects.
In addition, mututations in NPSR have been linked to a susceptibility to asthma (rs3249801, A107I). Hence NPSR has also been called GPRA (G protein-coupled receptor for asthma susceptibility). Activation of NPSR in the airway epithelium has a number of effects including upregulation of matrix metalloproteinases which are involved in the pathogenesis of asthma. It has been shown that activation of NPSR by NPS affects both gastrointestinal motility and mucosal permeability simultaneously. Aberrant signaling and upregulation of NPSR1 could potentially exacerbate dysmotility and hyperpermeability by local mechanisms in gastrointestinal functional and inflammatory reactions.
The very rare NPSR mutation Y206H, which makes the receptor more sensitive to NPS, is found in human families that need l |
https://en.wikipedia.org/wiki/Minicircle | Minicircles are small (~4kb) circular replicons. They occur naturally in some eukaryotic organelle genomes. In the mitochondria-derived kinetoplast of trypanosomes, minicircles encode guide RNAs for RNA editing. In Amphidinium, the chloroplast genome is made of minicircles that encode chloroplast proteins.
In vitro experimentally-derived minicircles
Minicircles are small (~4kb) circular plasmid derivatives that have been freed from all prokaryotic vector parts. They have been applied as transgene carriers for the genetic modification of mammalian cells, with the advantage that, since they contain no bacterial DNA sequences, they are less likely to be perceived as foreign and destroyed. (Typical transgene delivery methods involve plasmids, which contain foreign DNA.) The smaller size of minicircles also extends their cloning capacity and facilitates their delivery into cells.
Their preparation usually follows a two-step procedure:
production of a 'parental plasmid' (bacterial plasmid with eukaryotic inserts) in E. coli
induction of a site-specific recombinase at the end of this process but still in bacteria. These steps are followed by the
excision of prokaryotic vector parts via two recombinase-target sequences at both ends of the insert
recovery of the resulting minicircle (vehicle for the highly efficient modification of the recipient cell) and the miniplasmid by capillary gel electrophoresis (CGE)
The purified minicircle can be transferred into the recipient cell |
https://en.wikipedia.org/wiki/Neuropeptide%20B/W%20receptor | The neuropeptide B/W receptors are members of the G-protein coupled receptor superfamily of integral membrane proteins which bind the neuropeptides B and W. These receptors are predominantly expressed in the CNS and have a number of functions including regulation of the secretion of cortisol.
References
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Optical%20downconverter | Optical DownConverter (ODC) is an example of a non-linear optical process, in which two beams of light of different frequencies and interact, creating microwave with frequency . It is a generalization of microwave. In the latter, , both of which can be provided by a single light source. From a quantum mechanical perspective, ODC can be seen as result of differencing two photons to produce a microwave. Since the energy of a photon is given by
the frequency summing is simply a statement that energy is conserved.
In a common ODC application, light from a tunable infrared laser is combined with light from a fixed frequency visible laser to produce a microwave created by a wave mixing process.
The ODC use milimeteric microwave cavity that include photonic crystal that provide by two signal frequency light source. The microwave is detected by the cavity antenna.
See also
Sum-frequency generation
Homodyne detection
External links
Frequency Measurement
AdvR - Down conversion in KTiOPO4 (KTP)
Nonlinear optics |
https://en.wikipedia.org/wiki/DNA%20analyzer | A DNA analyzer is a device used to determine characteristics of a person's DNA. For example, genetic fingerprinting can be conducted with a portable DNA analyzer.
References
DNA |
https://en.wikipedia.org/wiki/Neuropeptide%20FF%20receptor | The neuropeptide FF receptors are members of the G-protein coupled receptor superfamily of integral membrane proteins which bind the pain modulatory neuropeptides AF and FF.
The Neuropeptide FF receptor family is a member of the G protein-coupled receptor superfamily containing two subtypes, NPFF1 and NPFF2, which exhibit a high affinity for Neuropeptide FF (NPFF) peptides. NPFF1 is broadly distributed in the central nervous system with the highest levels found in the limbic system and the hypothalamus. NPFF2 is present in high density, particularly in mammals in the superficial layers of the spinal cord where it is involved in nociception and modulation of opioid functions. These receptors participate to the modulation of opioid receptor function in the brain and spinal cord, and can either reduce or increase opioid receptor function depending which tissue they are released in, reflecting a complex role for neuropeptide FF in pain responses.
NPFF receptors are coupled to G proteins and regulate adenylyl cyclase in recombinant cell lines (CHO, HEK 293, SH-SY5Y). NPFF receptors are also coupled to voltage-gated N-type Ca2+ channels.
Ligands
Agonists
Neuropeptide AF
Neuropeptide FF
Neuropeptide SF (RFRP-1)
Neuropeptide VF (RFRP-3)
Antagonists
BIBP-3226 (mixed NPFF1 / NPY1 antagonist)
RF-9
References
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPCR%20neuropeptide%20receptor | GPCR neuropeptide receptors are G-protein coupled receptors which bind various neuropeptides. Members include:
Neuropeptide B/W receptor
NPBWR1
NPBWR2
Neuropeptide FF receptor
NPFFR1
NPFFR2
Neuropeptide S receptor
NPSR1
Neuropeptide Y receptor
Y1 - NPY1R
Y2 - NPY2R
Y4 - PPYR1
Y5 - NPY5R
References
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Wilms%20tumor%20protein | Wilms tumor protein (WT33) is a protein that in humans is encoded by the WT1 gene on chromosome 11p.
Function
This gene encodes a transcription factor that contains four zinc finger motifs at the C-terminus and a proline / glutamine-rich DNA-binding domain at the N-terminus. It has an essential role in the normal development of the urogenital system, and it is mutated in a subset of patients with Wilms' tumor, the gene's namesake. Multiple transcript variants, resulting from alternative splicing at two coding exons, have been well characterized. There is also evidence for the use of non-AUG (CUG) translation initiation site upstream of, and in-frame with the first AUG, leading to additional isoforms.
Structure
The WT1 gene product shows similarity to the zinc fingers of the mammalian growth regulated early growth response protein 1 (EGR1) and (EGR2) proteins.
Clinical significance
Mutations of Wilms' tumor suppressor gene1 (WT1) are associated with embryonic malignancy of the kidney, affecting around 1-9 in 100,000 infants. It occurs in both sporadic and hereditary forms. Inactivation of WT1 causes Wilms tumour, and Denys-Drash syndrome (DDS), leading to nephropathy and genital abnormalities. The WT1 protein has been found to bind a host of cellular factors, e.g. p53, a known tumor suppressor. Despite the name, WT1 mutation is found in only about 5-10% of Wilms Tumor cases. Some other genes associated with this disease are BRCA2 and GPC3
WT1 is mutated in a mutuall |
https://en.wikipedia.org/wiki/Calmodulin%201 | Calmodulin 1 is a protein that in humans is encoded by the CALM1 gene.
Function
Calmodulin 1 is the archetype of the family of calcium-modulated (calmodulin) proteins of which nearly 20 members have been found. They are identified by their occurrence in the cytosol or on membranes facing the cytosol and by a high affinity for calcium. Calmodulin contains 149 amino acids and has 4 calcium-binding EF hand motifs. Its functions include roles in growth and the cell cycle as well as in signal transduction and the synthesis and release of neurotransmitters.
Interactions
Calmodulin 1 has been shown to interact with:
AKAP9,
Androgen receptor,
IQGAP1,
PPEF1, and
TRPV1.
References
Further reading
External links
UniProt. Calm1 Human Gene
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/Retinoid%20X%20receptor%20alpha | Retinoid X receptor alpha (RXR-alpha), also known as NR2B1 (nuclear receptor subfamily 2, group B, member 1) is a nuclear receptor that in humans is encoded by the RXRA gene.
Function
Retinoid X receptors (RXRs) and retinoic acid receptors (RARs), are nuclear receptors that mediate the biological effects of retinoids by their involvement in retinoic acid-mediated gene activation. These receptors exert their action by binding, as homodimers or heterodimers, to specific sequences in the promoters of target genes and regulating their transcription. The protein encoded by this gene is a member of the steroid and thyroid hormone receptor superfamily of transcription factors. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the cytochrome P450 system genes.
Interactive pathway map
Interactions
Retinoid X receptor alpha has been shown to interact with:
BCL3,
BRD8,
CLOCK,
FXR
IGFBP3,
ITGB3BP,
LXR-β,
MyoD,
NCOA6,
NFKBIB,
NPAS2,
NRIP1,
NR4A1,
NCOA2,
NCOA3,
POU2F1,
PPARGC1A,
PPAR-γ,
RNF8,
RAR-α,
SHP,
TADA3L,
TBP,
TRIM24,
TR-β, and
|
https://en.wikipedia.org/wiki/Actin%2C%20alpha%20skeletal%20muscle | Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1 gene.
Actin alpha 1 which is expressed in skeletal muscle is one of six different actin isoforms which have been identified. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.
Skeletal actin gene expression
Skeletal alpha actin expression is induced by stimuli and conditions known to cause muscle formation. Such conditions result in fusion of committed cells (satellite cells) into myotubes, to form muscle fibers. Skeletal actin itself, when expressed, causes expression of several other "myogenic genes", which are essential to muscle formation. One key transcription factor that activates skeletal actin gene expression is Serum Response Factor ("SRF"), a protein that binds to specific sites on the promoter DNA of the actin gene. SRF may bring a number of other proteins to the promoter of skeletal actin, such as androgen receptor, and thereby contribute to induction of skeletal actin gene expression by androgenic (often termed "anabolic") steroids.
Interactions
Actin, alpha 1 has been shown to interact with TMSB4X, MIB2 and PRKCE.
Clinical significance
Mutations in the ACTA1 gene are known to cause the following conditions:
Nemaline myopathy 3 (NEM3);
Myopathy, actin, congenital, with excess of thin myofilaments (MPCETM);
Myopathy, congenital, with fiber-type disproportion (CF |
https://en.wikipedia.org/wiki/CTSS | CTSS may refer to:
Cathepsin S, a human enzyme
Center for Terrorism & Security Studies at UMass Lowell, US
Clementi Town Secondary School, Singapore
Compatible Time-Sharing System, a computer operating system
Cray Time Sharing System, a computer operating centre |
https://en.wikipedia.org/wiki/CHEK1 | Checkpoint kinase 1, commonly referred to as Chk1, is a serine/threonine-specific protein kinase that, in humans, is encoded by the CHEK1 gene. Chk1 coordinates the DNA damage response (DDR) and cell cycle checkpoint response. Activation of Chk1 results in the initiation of cell cycle checkpoints, cell cycle arrest, DNA repair and cell death to prevent damaged cells from progressing through the cell cycle.
Discovery
In 1993, Beach and associates initially identified Chk1 as a serine/threonine kinase which regulates the G2/M phase transition in fission yeast. Constitutive expression of Chk1 in fission yeast was shown to induce cell cycle arrest. The same gene called Rad27 was identified in budding yeast by Carr and associates. In 1997, homologs were identified in more complex organisms including the fruit fly, human and mouse. Through these findings, it is apparent Chk1 is highly conserved from yeast to humans.
Structure
Human Chk1 is located on chromosome 11 on the cytogenic band 11q22-23. Chk1 has a N-terminal kinase domain, a linker region, a regulatory SQ/TQ domain and a C-terminal domain. Chk1 contains four Ser/Gln residues. Chk 1 activation occurs primarily through the phosphorylation of the conserved sites, Ser-317, Ser-345 and less often at Ser-366.
Function
Checkpoint kinases (Chks) are protein kinases that are involved in cell cycle control. Two checkpoint kinase subtypes have been identified, Chk1 and Chk2. Chk1 is a central component of genome surveillance pa |
https://en.wikipedia.org/wiki/FHIT | Bis(5'-adenosyl)-triphosphatase also known as fragile histidine triad protein (FHIT) is an enzyme that in humans is encoded by the FHIT gene.
Function
FHIT is also known as human accelerated region 10. It may, therefore, have played a key role in differentiating humans from apes.
This gene, a member of the histidine triad gene family, encodes a diadenosine
P1,P3-bis(5'-adenosyl)-triphosphate adenylohydrolase involved in purine metabolism. The gene encompasses the common fragile site FRA3B on chromosome 3, where carcinogen-induced damage can lead to translocations and aberrant transcripts of this gene. In fact, aberrant transcripts from this gene have been found in about half of all esophageal, stomach, and colon carcinomas.
Though the exact molecular function of FHIT is still partially unclear, the gene works as a tumor suppressor as it has been demonstrated in animal studies. Furthermore FHIT has been shown to synergize with VHL, another tumor suppressor, in protecting against chemically - induced lung cancer.
FHIT also acts as a tumor suppressor of HER2/neu driven breast cancer.
Interactions
FHIT has been shown to interact with UBE2I.
References
External links |
https://en.wikipedia.org/wiki/Surface%20gradient | In vector calculus, the surface gradient is a vector differential operator that is similar to the conventional gradient. The distinction is that the surface gradient takes effect along a surface.
For a surface in a scalar field , the surface gradient is defined and notated as
where is a unit normal to the surface. Examining the definition shows that the surface gradient is the (conventional) gradient with the component normal to the surface removed (subtracted), hence this gradient is tangent to the surface. In other words, the surface gradient is the orthographic projection of the gradient onto the surface.
The surface gradient arises whenever the gradient of a quantity over a surface is important. In the study of capillary surfaces for example, the gradient of spatially varying surface tension doesn't make much sense, however the surface gradient does and serves certain purposes.
See also
Aspect (geography)
Geomorphometry#Surface gradient Derivatives
Grade (slope)
Spatial gradient
References
Vector calculus
Surfaces
Vector physical quantities |
https://en.wikipedia.org/wiki/Importin%20subunit%20alpha-1 | Importin subunit alpha-1 is a protein that in humans is encoded by the KPNA2 gene.
The import of proteins into the nucleus is a process that involves at least 2 steps. The first is an energy-independent docking of the protein to the nuclear envelope and the second is an energy-dependent translocation through the nuclear pore complex. Imported proteins require a nuclear localization sequence (NLS) which generally consists of a short region of basic amino acids or 2 such regions spaced about 10 amino acids apart. Proteins involved in the first step of nuclear import are members of the alpha importin family of karyopherins such as importin subunit alpha-1. These include the Xenopus protein importin and its yeast homolog, SRP1 (a suppressor of certain temperature-sensitive mutations of RNA polymerase I in Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V(D)J recombination
Interactions
Karyopherin alpha 2 has been shown to interact with:
ARL4A
ITK,
KPNB1,
PLAG1,
RECQL, and
SGK.
References
Further reading
Armadillo-repeat-containing proteins |
https://en.wikipedia.org/wiki/TOP2A | DNA topoisomerase IIα is a human enzyme encoded by the TOP2A gene.
Topoisomerase IIα relieves topological DNA stress during transcription, condenses chromosomes, and separates chromatids. It catalyzes the transient breaking and rejoining of two strands of duplex DNA which allows the strands to pass through one another. Two forms of this enzyme exist as likely products of a gene duplication event. The gene encoding this form, alpha, is localized to chromosome 17 and the beta gene is localized to chromosome 3. The gene encoding this enzyme functions as the target for several chemotherapy agents and a variety of mutations in this gene have been associated with the development of drug resistance. Reduced activity of this enzyme may also play a role in ataxia-telangiectasia.
Interactions
TOP2A has been shown to interact with SMURF2, HDAC1, CDC5L, Small ubiquitin-related modifier 1, P53, and TOPBP1.
In other species
In Drosophila Hadlaczky et al 1988 found DNA topoisomerase II α to correlate with cell proliferation - but β did not.
See also
Topoisomerase II
TOP2B - Topoisomerase II beta
Gene duplication
Ataxia-telangiectasia
TOPBP1
References
Further reading |
https://en.wikipedia.org/wiki/PPARGC1A | Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α) is a protein that in humans is encoded by the PPARGC1A gene. PPARGC1A is also known as human accelerated region 20 (HAR20). It may, therefore, have played a key role in differentiating humans from apes.
PGC-1α is the master regulator of mitochondrial biogenesis. PGC-1α is also the primary regulator of liver gluconeogenesis, inducing increased gene expression for gluconeogenesis.
Function
PGC-1α is a gene that contains two promoters, and has 4 alternative splicings. PGC-1α is a transcriptional coactivator that regulates the genes involved in energy metabolism. It is the master regulator of mitochondrial biogenesis. This protein interacts with the nuclear receptor PPAR-γ, which permits the interaction of this protein with multiple transcription factors. This protein can interact with, and regulate the activity of, cAMP response element-binding protein (CREB) and nuclear respiratory factors (NRFs) . PGC-1α provides a direct link between external physiological stimuli and the regulation of mitochondrial biogenesis, and is a major factor causing slow-twitch rather than fast-twitch muscle fiber types.
Endurance exercise has been shown to activate the PGC-1α gene in human skeletal muscle. Exercise-induced PGC-1α in skeletal muscle increases autophagy and unfolded protein response.
PGC-1α protein may also be involved in controlling blood pressure, regulating cellular cholesterol homeostasis, and the d |
https://en.wikipedia.org/wiki/T-cell%20surface%20glycoprotein%20CD3%20zeta%20chain | T-cell surface glycoprotein CD3 zeta chain also known as T-cell receptor T3 zeta chain or CD247 (Cluster of Differentiation 247) is a protein that in humans is encoded by the CD247 gene.
Some older literature mention a similar protein called "CD3 eta" in mice. It is now understood to be an isoform differing in the last exon.
Genomics
The gene is located on the long arm of chromosome 1 at location 1q22-q25 on the Crick (negative) strand. The encoded protein is 164 amino acids long with a predicted weight of 18.696 kiloDaltons.
Function
T-cell receptor zeta (ζ), together with T-cell receptor alpha/beta and gamma/delta heterodimers and CD3-gamma, -delta, and -epsilon, forms the T-cell receptor-CD3 complex. The zeta chain plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. Low expression of the antigen results in impaired immune response. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
Interactions
CD247 has been shown to interact with Janus kinase 3 and Protein unc-119 homolog.
See also
Cluster of differentiation
ZAP70
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/Ku70 | Ku70 is a protein that, in humans, is encoded by the XRCC6 gene.
Function
Together, Ku70 and Ku80 make up the Ku heterodimer, which binds to DNA double-strand break ends and is required for the non-homologous end joining (NHEJ) pathway of DNA repair. It is also required for V(D)J recombination, which utilizes the NHEJ pathway to promote antigen diversity in the mammalian immune system.
In addition to its role in NHEJ, Ku is also required for telomere length maintenance and subtelomeric gene silencing.
Ku was originally identified when patients with systemic lupus erythematosus were found to have high levels of autoantibodies to the protein.
Aging
Mouse embryonic stem cells with homozygous Ku70 mutations, that is Ku70−/− cells, have markedly increased sensitivity to ionizing radiation compared to heterozygous Ku70+/− or wild-type Ku70+/+ embryonic stem cells. Mutant mice deficient in Ku70 exhibit early aging. Using several specific criteria of aging, the mutant mice were found to display the same aging signs as control mice, but at a considerably earlier chronological age. These results suggest that reduced ability to repair DNA double-strand breaks causes early aging, and that the wild-type Ku70 gene plays an important role in longevity assurance. (Also see DNA damage theory of aging.)
Clinical
A mutation in this gene has been described in a set of 24 families with autism. While this is suggestive that this gene may play a role in the development of autism, furth |
https://en.wikipedia.org/wiki/Integrin%20alpha%202b | Integrin alpha-IIb is a protein that in humans is encoded by the ITGA2B gene. ITGA2B, also known as CD41, encodes integrin alpha chain 2b. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain 2b undergoes post-translational cleavage to yield disulfide-linked light and heavy chains that join with beta 3 to form a fibrinogen receptor expressed in platelets that plays a crucial role in coagulation. Mutations that interfere with this role result in thrombasthenia. At least 38 disease-causing mutations in this gene have been discovered. In addition to adhesion, integrins are known to participate in cell-surface mediated signalling.
Interactions
ITGA2B has been shown to interact with AUP1 and CLNS1A.
See also
Cluster of differentiation
Glycoprotein IIb/IIIa
References
Further reading
External links
Clusters of differentiation
Integrins |
https://en.wikipedia.org/wiki/TIMP2 | Tissue inhibitor of metalloproteinases 2 (TIMP2) is a gene and a corresponding protein. The gene is a member of the TIMP gene family. The protein is thought to be a metastasis suppressor.
Function
The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases (MMP), a group of peptidases involved in degradation of the extracellular matrix. In addition to an inhibitory role against metalloproteinases, the encoded protein has a unique role among TIMP family members in its ability to directly suppress the proliferation of endothelial cells. As a result, the encoded protein may be critical to the maintenance of tissue homeostasis by suppressing the proliferation of quiescent tissues in response to angiogenic factors, and by inhibiting protease activity in tissues undergoing remodelling of the extracellular matrix. TIMP2 functions as both an MMP inhibitor and an activator. TIMPs inhibit active MMPs, but different TIMPs inhibit different MMPs better than others. For example, TIMP-1 inhibits MMP-7, MMP-9, MMP-1 and MMP-3 better than TIMP-2, and TIMP-2 inhibits MMP-2 more effectively than other TIMPs.
In melanocytic cells TIMP2 gene expression may be regulated by MITF.
A more recent discovery is that TIMP2 plays an important role in hippocampal function and cognitive function. It plays a critical role in the benefit conferred to old mice when given human umbilical cord blood.
Interactions
TIMP2 has been shown to interact with:
MMP14 and
MM |
https://en.wikipedia.org/wiki/Capillary%20surface | In fluid mechanics and mathematics, a capillary surface is a surface that represents the interface between two different fluids. As a consequence of being a surface, a capillary surface has no thickness in slight contrast with most real fluid interfaces.
Capillary surfaces are of interest in mathematics because the problems involved are very nonlinear and have interesting properties, such as discontinuous dependence on boundary data at isolated points. In particular, static capillary surfaces with gravity absent have constant mean curvature, so that a minimal surface is a special case of static capillary surface.
They are also of practical interest for fluid management in space (or other environments free of body forces), where both flow and static configuration are often dominated by capillary effects.
The stress balance equation
The defining equation for a capillary surface is called the stress balance equation, which can be derived by considering the forces and stresses acting on a small volume that is partly bounded by a capillary surface. For a fluid meeting another fluid (the "other" fluid notated with bars) at a surface , the equation reads
where is the unit normal pointing toward the "other" fluid (the one whose quantities are notated with bars), is the stress tensor (note that on the left is a tensor-vector product), is the surface tension associated with the interface, and is the surface gradient. Note that the quantity is twice the mean curvature of the su |
https://en.wikipedia.org/wiki/ETS1 | Protein C-ets-1 is a protein that in humans is encoded by the ETS1 gene. The protein encoded by this gene belongs to the ETS family of transcription factors.
Function
There are 28 ETS genes in humans and 27 in mice. They bind the DNA via their winged-helix-turn-helix DNA binding motif known as the Ets domain that specifically recognizes DNA sequences that contain a GGAA/T core element. However, Ets proteins differ significantly in their preference for the sequence flanking the GGAA/T core motif. For instance, the consensus sequence for Ets1 is PuCC/a-GGAA/T-GCPy. On the other hand, many natural Ets1-responsive GGAA/T elements differ from this consensus sequence. The later suggests that several other transcription factors may facilitate Ets1 binding to unfavorable DNA sequences. ChIP-Seq studies have shown that Ets1 can bind both AGGAAG and CGGAAG motifs.
Ets1 binds to DNA as a monomer. Phosphorylation of serine residues of the C-terminal domain (in the nucleotide sequence they belong to exon VII) known as autoinhibition makes Ets1 inactive. There are several ways to activate Ets1. First, Ets1 can be dephosphorylated. Second, two Ets1 can be activated If two Ets molecules homodimerize. The homodimerization occurs if DNA binding sites are present in the correct orientation and spacing. Thus, the exact layout of binding sites within an enhancer or promoter segment to either relieve or allow autoinhibition of Ets1 to occur may strongly influence whether or not Ets1 actually |
https://en.wikipedia.org/wiki/GJB1 | Gap junction beta-1 protein (GJB1), also known as connexin 32 (Cx32), is a transmembrane protein that in humans is encoded by the GJB1 gene. Gap junction beta-1 protein is a member of the gap junction connexin family of proteins that regulates and controls the transfer of communication signals across cell membranes, primarily in the liver and peripheral nervous system. However, the protein is expressed in multiple organs, including in oligodendrocytes in the central nervous system.
Mutations of the GJB1 gene affecting the signalling of and trafficking through gap junctions, resulting in an inherited peripheral neuropathy called X-linked Charcot-Marie-Tooth Disease. Complications include the demyelination of oligodendrocytes and Schwann cells, causing delayed transmission rates of nerve communication in the peripheral nervous system, due to irregularities in the normal function of the cells. This condition leads to a number of symptoms, most commonly muscle weakness and sensory problems in the outer extremities of the limbs. As a result, muscle atrophy and soft tissue injuries due to delayed nerve transmission can occur. In males, due to the hemizygousity of the X-chromosome, the symptoms and issues surrounding X-linked Charcot-Marie-Tooth disease are more prevalent.
Function
Connexins are membrane-spanning proteins that assemble to form gap junction channels that facilitate the transfer of ions and small molecules between cells. For a general discussion of connexin protei |
https://en.wikipedia.org/wiki/Ezrin | Ezrin also known as cytovillin or villin-2 is a protein that in humans is encoded by the EZR gene.
Structure
The N-terminus of ezrin contains a FERM domain which is further subdivided into three subdomains. The C-terminus contain an ERM domain.
Function
The cytoplasmic peripheral protein encoded by this gene can be phosphorylated by protein-tyrosine kinase in microvilli and is a member of the ERM protein family. This protein serves as a linker between plasma membrane and actin cytoskeleton. It plays a key role in cell surface structure adhesion, migration, and organization.
The N-terminal domain (also called FERM domain) binds sodium-hydrogen exchanger regulatory factor (NHERF) protein (involving long-range allostery). This binding can happen only when ezrin is in its active state. The activation of ezrin occurs in synergism of the two factors: 1) binding of the N-terminal domain to phosphatidylinositol(4,5)bis-phosphate (PIP2) and 2) phosphorylation of threonine T567 in the C-terminal domain. Binding to actin filaments (via C-terminal) and to membrane proteins (via N-terminal) stabilizes the protein's conformation in its active mode. The membrane proteins like CD44 and ICAM-2 are indirect binding partners of ezrin, while EBP50 (ERM binding protein 50) can associate with ezrin directly.
Interactions
VIL2 has been shown to interact with:
CD43,
FASLG,
ICAM-1,
ICAM2,
ICAM3,
Merlin,
MSN,
PIK3R1,
PALLD
S100P,
SDC2,
SLC9A3R1,
SLC9A3R2, and
VC |
https://en.wikipedia.org/wiki/XPO1 | Exportin 1 (XPO1), also known as chromosomal region maintenance 1 (CRM1), is a eukaryotic protein that mediates the nuclear export of various proteins and RNAs.
History
XPO1 (CRM1) originally was identified in the fission yeast Schizosaccharomyces pombe in a genetic screen, and investigators determined that it was involved in control of the chromosome structure. It was later shown to be the nuclear transport receptor for cargos with leucine-rich nuclear export signals (NES). The structural details of the interaction of XPO1 with its cargos were revealed two decades after the gene was identified.
Function
XPO1 mediates NES-dependent protein transport. It exports several hundreds of different proteins from the nucleus. XPO1 is involved in the nuclear export of ribosomal subunits. XPO1 plays a role in export of various RNAs including U snRNAs, rRNAs (as a part of ribosomal subunits), and some mRNAs.
Medical relevance
XPO1 is involved in various viral infections. For example, it is required for the nuclear export of HIV-1 RNA in complex with the viral protein Rev, an event that is a crucial part of the infection cycle. XPO1 is affected in some cancer types and is therefore viewed as a target for development of anti-cancer drugs. Selinexor, a drug specifically targeting XPO1, was approved by the FDA for treatment of multiple myeloma.
Interactions
XPO1 has been shown to interact with:
APC,
CDKN1B,
CIITA,
NMD3,
Nucleoporin 62,
RANBP1,
RANBP3,
Ran,
SMARCB |
https://en.wikipedia.org/wiki/National%20Matching%20Service | National Matching Services (NMS) specializes in the development and administration of Matching Programs. NMS was founded in 1985, after developing sophisticated matching algorithms and software for the placement of physicians into residencies in the US. Since then, NMS has implemented Matching Programs in a number of industries and professions, including osteopathic medicine, psychology, dentistry, pharmacy, and optometry. NMS is headquartered in Toronto.
Matching Programs place applicants into positions based on lists of preferred choices submitted by applicants and recruiters. A Matching Program eliminates premature decisions based on incomplete information by allowing all offers, acceptances or rejections to occur at the same time. Therefore many common adverse situations are eliminated from the recruitment process, such as applicants hoarding multiple offers, applicants reneging on a prior acceptance in order to accept a more preferred subsequent offer, and recruiters overfilling the number of positions available. Applicants and recruiters benefit from having full choice of all potential placements. The best strategy for both applicants and recruiters is to submit preference lists that reflect their true preferences.
References
Employment agencies of Canada
Medical education in the United States
Public employment service
Medical and health organizations based in Ontario
Stable matching |
https://en.wikipedia.org/wiki/N-acetyltransferase%202 | N-acetyltransferase 2 (arylamine N-acetyltransferase), also known as NAT2, is an enzyme which in humans is encoded by the NAT2 gene.
Function
This gene encodes a type of N-acetyltransferase. The NAT2 isozyme functions to both activate and deactivate arylamine and hydrazine drugs and carcinogens. Polymorphisms in this gene are responsible for the N-acetylation polymorphism in which human populations segregate into rapid, intermediate, and slow acetylator phenotypes. Polymorphisms in NAT2 are also associated with higher incidences of cancer and drug toxicity. A second arylamine N-acetyltransferase gene (NAT1) is located near NAT2.
Phenotype prediction
The NAT2 acetylator phenotype can be inferred from NAT2 genotype (a combination of SNPs observed in a given individual).
References
Further reading
External links
The Arylamine N-acetyltransferase Gene Nomenclature Committee homepage
PDBe-KB provides an overview of all the structure information available in the PDB for Human Arylamine N-acetyltransferase 2
Human proteins |
https://en.wikipedia.org/wiki/Juang%20language | The Juang language is a Munda language of the Austroasiatic language family spoken primarily by the Juang people of Odisha state, eastern India.
Classification
The Juang language belongs to the Munda language family, the whole of which is classified as a branch of the greater Austroasiatic language family. Among the Munda languages, Juang is considered to be most closely related to Kharia, although Anderson considers Juang and Kharia to have split off from each other relatively early.
Juang can be roughly divided into the Hill and Plains varieties, both of which are spoken in Odisha (Patnaik 2008:508).
Hill Juang: Gonasika Hills (in Keonjhar district) and Pallara Hills
Plains Juang: about 147 villages in southern Keonjhar district and eastern Dhenkanal district
Distribution
Juang is spoken by about 30,875 people according to the 2001 Indian census, 65% of ethnic population In Odisha state, it is spoken in southern Keonjhar district, northern Angul district, and eastern Dhenkanal district (Patnaik 2008:508).
Juang is currently an Endangered language and is considered to vulnerable, or (not spoken by children outside of home).
Juang currently has roughly under 20,000 speakers remaining
Grammar
In Juang a number of roots are clearly exempt from the Transitive verb/Intransitive verb opposition, so that the function of the root can be determined only from its co-occurrence with the particular set of tense markers.
For Example,
pag- Set I 'to break' -Set II 'to be broken1 |
https://en.wikipedia.org/wiki/Fibrinogen%20gamma%20chain | Fibrinogen gamma chain, also known as fibrinogen gamma gene (FGG), is a human gene found on chromosome 3.
The protein encoded by this gene is the gamma component of fibrinogen, a blood-borne glycoprotein composed of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia and thrombophilia. Alternative splicing of the mRNA chain results in two transcript variants; the common γA chain and the alternatively spliced γ' chain. Approximately 10% of the total plasma fibrinogen consists of γA/γ' fibrinogen, with <1% consisting of γ'/γ' fibrinogen. Increased and decreased levels of γA/γ' fibrinogen have been associated with coronary artery disease and deep vein thrombosis respectively.
In the lung parenchyma of smokers, upregulation of FGG transcript levels has been reported.
References
Further reading |
https://en.wikipedia.org/wiki/Histone%20deacetylase%202 | Histone deacetylase 2 (HDAC2) is an enzyme that in humans is encoded by the HDAC2 gene. It belongs to the histone deacetylase class of enzymes responsible for the removal of acetyl groups from lysine residues at the N-terminal region of the core histones (H2A, H2B, H3, and H4). As such, it plays an important role in gene expression by facilitating the formation of transcription repressor complexes and for this reason is often considered an important target for cancer therapy.
Though the functional role of the class to which HDAC2 belongs has been carefully studied, the mechanism by which HDAC2 interacts with histone deacetylases of other classes has yet to be elucidated. HDAC2 is broadly regulated by protein kinase 2 (CK2) and protein phosphatase 1 (PP1), but biochemical analysis suggests its regulation is more complex (evinced by the coexistence of HDAC1 and HDAC2 in three distinct protein complexes). Essentially, the mechanism by which HDAC2 is regulated is still unclear by virtue of its various interactions, though a mechanism involving p300/CBP-associated factor and HDAC5 has been proposed in the context of cardiac reprogramming.
Generally, HDAC2 is considered a putative target for the treatment for a variety of diseases, due to its involvement in cell cycle progression. Specifically, HDAC2 has been shown to play a role in cardiac hypertrophy, Alzheimer's disease, Parkinson's disease, acute myeloid leukemia (AML), osteosarcoma, and stomach cancer.
Structure and mechan |
https://en.wikipedia.org/wiki/HMGB1 | High mobility group box 1 protein, also known as high-mobility group protein 1 (HMG-1) and amphoterin, is a protein that in humans is encoded by the HMGB1 gene.
HMG-1 belongs to the high mobility group and contains a HMG-box domain.
Function
Like the histones, HMGB1 is among the most important chromatin proteins. In the nucleus HMGB1 interacts with nucleosomes, transcription factors, and histones. This nuclear protein organizes the DNA and regulates transcription. After binding, HMGB1 bends DNA, which facilitates the binding of other proteins. HMGB1 supports transcription of many genes in interactions with many transcription factors. It also interacts with nucleosomes to loosen packed DNA and remodel the chromatin. Contact with core histones changes the structure of nucleosomes.
The presence of HMGB1 in the nucleus depends on posttranslational modifications. When the protein is not acetylated, it stays in the nucleus, but hyperacetylation on lysine residues causes it to translocate into the cytosol.
HMGB1 has been shown to play an important role in helping the RAG endonuclease form a paired complex during V(D)J recombination.
Role in inflammation
HMGB1 is secreted by immune cells (like macrophages, monocytes and dendritic cells) through leaderless secretory pathway. Activated macrophages and monocytes secrete HMGB1 as a cytokine mediator of Inflammation. Antibodies that neutralize HMGB1 confer protection against damage and tissue injury during arthritis, colitis, isc |
https://en.wikipedia.org/wiki/MMP7 | Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene. The enzyme () has also been known as matrin, putative (or punctuated) metalloproteinase-1, matrix metalloproteinase pump 1, PUMP-1 proteinase, PUMP, metalloproteinase pump-1, putative metalloproteinase, MMP). Human MMP-7 has a molecular weight around 30 kDa.
Matrilysin was discovered by Sellers and Woessner in the uterus of the rat in 1988. The complementary DNA (cDNA) of human MMP7 was isolated in 1988 by Muller et al. MMP7 is a member of the matrix metalloproteinase (MMP) family consisting of structural-related zinc-dependent endopeptidases. The primary role of cleaved/activated MMP7 is to break down extracellular matrix by degrading macromolecules including casein, type I, II, IV, and V gelatins, fibronectin, and proteoglycan.
Gene, regulation, and expression
The human MMP7 is located on chromosome 11 q22.3. MMP genes are clustered in q region of human Chromosome 11 including matrilysin, collagenase-1, stromelysin1, stromelysin-2, and metalloelastase genes. It consists of 267 amino acids. The cDNA of MMP7 is 49% homologous to stromelysin-1. Comparing to other members of MMP family, MMP7 does not have a C-terminal protein domain.
The promoter of the human MMP7 contains a TATA box, an activator protein 1 (AP-1) site, and two inverted polyomavirus enhancer A-binding proteins 2 (PEA-3). The AP-1/PEA- |
https://en.wikipedia.org/wiki/Bookie%20Bolin | Treva Gene "Bookie" Bolin (born June 17, 1940) is a former American football offensive lineman who played professional in the National Football League (NFL) from 1962 through 1969. He played college football at the University of Mississippi where he was part of the 1960 national championship team, and he attended Okolona High School.
References
1940 births
Living people
American football offensive linemen
Minnesota Vikings players
New York Giants players
Ole Miss Rebels football players
People from Hamilton, Alabama
Players of American football from Alabama |
https://en.wikipedia.org/wiki/Effusion%20%28disambiguation%29 | Effusion is the process of gases passing through a small hole.
Effusion may also refer to:
Medicine
The seeping of fluid into a body cavity, the fluid itself, or an abnormal collection of fluid in a body cavity or space:
Ascites
Pericardial effusion
Pleural effusion
Joint effusion
Subdural Effusion
Mastoid Effusion
Knee effusion
Sometimes called "hydrops"
Geology
Effusive eruption, an effusion of lava from a volcano |
https://en.wikipedia.org/wiki/SKP2 | S-phase kinase-associated protein 2 is an enzyme that in humans is encoded by the SKP2 gene.
Structure and function
Skp2 contains 424 residues in total with the ~40 amino acid F-box domain lying closer to the N-terminal region at the 94-140 position and the C-terminal region forming a concave surface consisting of ten leucine-rich repeats (LRRs). The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which often—but not always—recognize substrates in a phosphorylation-dependent manner. In this SCF complex, Skp2 acts as the substrate recognition factor.
F-box Domain
The F-box proteins are divided into three classes: Fbxws containing WD40 repeat domains, Fbxls containing leucine-rich repeats, and Fbxos containing either different protein–protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxls class.
In addition to an F-box, this protein contains 10 tandem leucine-rich repeats. Alternative splicing of this gene generates 2 transcript variants encoding different isoforms. After the tenth LRR, the ~30-residue C-terminal tail turns back towards the first LRR, forming what has been referred to as a ‘safety-belt’ that might aid to pin down substrates into the concave surface formed by the LRRs.
Skp2 forms a stable complex with the cyclin A-CDK2 S-phase kinase. It specifically recognizes and promotes the degradation of phosphorylated cyclin-dependent kinase in |
https://en.wikipedia.org/wiki/TCF3 | Transcription factor 3 (E2A immunoglobulin enhancer-binding factors E12/E47), also known as TCF3, is a protein that in humans is encoded by the TCF3 gene. TCF3 has been shown to directly enhance Hes1 (a well-known target of Notch signaling) expression.
Function
This gene encodes a member of the E protein (class I) family of helix-loop-helix transcription factors. The 9aaTAD transactivation domains of E proteins and MLL are very similar and both bind to the KIX domain of general transcriptional mediator CBP. E proteins activate transcription by binding to regulatory E-box sequences on target genes as heterodimers or homodimers, and are inhibited by heterodimerization with inhibitor of DNA-binding (class IV) helix-loop-helix proteins. E proteins play a critical role in lymphopoiesis, and the encoded protein is required for B and T lymphocyte development.
This gene regulates many developmental patterning processes such as lymphocyte and central nervous system (CNS) development. E proteins are involved in the development of lymphocytes. They initiate transcription by binding to regulatory E-box sequences on target genes.
Clinical significance
Deletion of this gene or diminished activity of the encoded protein may play a role in lymphoid malignancies. This gene is also involved in several chromosomal translocations that are associated with lymphoid malignancies including pre-B-cell acute lymphoblastic leukemia (t(1;19), with PBX1 and t(17;19), with HLF), childhood leukemia |
https://en.wikipedia.org/wiki/ZNF35 | Zinc finger protein 35 is a protein that in humans is encoded by the ZNF35 gene.
See also
Zinc finger
References
External links
Transcription factors |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.