source stringlengths 32 209 | text stringlengths 18 1.5k |
|---|---|
https://en.wikipedia.org/wiki/N6-methyl-lysine%20oxidase | In enzymology, a N6-methyl-lysine oxidase () is an enzyme that catalyzes the chemical reaction
N6-methyl-L-lysine + H2O + O2 L-lysine + formaldehyde + H2O2
The 3 substrates of this enzyme are N6-methyl-L-lysine, H2O, and O2, whereas its 3 products are L-lysine, formaldehyde, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is N6-methyl-L-lysine:oxygen oxidoreductase (demethylating). Other names in common use include epsilon-alkyl-L-lysine:oxygen oxidoreductase, N6-methyllysine oxidase, epsilon-N-methyllysine demethylase, epsilon-alkyllysinase, and 6-N-methyl-L-lysine:oxygen oxidoreductase (demethylating).
References
EC 1.5.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/NADPH%E2%80%94cytochrome-c2%20reductase | In enzymology, a NADPH—cytochrome-c2 reductase () is an enzyme that catalyzes the chemical reaction
NADPH + 2 ferricytochrome c2 NADP+ + H+ + 2 ferrocytochrome c2
Thus, the two substrates of this enzyme are NADPH and ferricytochrome c2, whereas its 3 products are NADP+, H+, and ferrocytochrome c2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a heme protein as acceptor. The systematic name of this enzyme class is NADPH:ferricytochrome-c2 oxidoreductase. Other names in common use include cytochrome c2 reductase (reduced nicotinamide adenine dinucleotide, phosphate), cytochrome c2 reductase (reduced nicotinamide adenine dinucleotide, and phosphate, NADPH). It employs one cofactor, FAD.
References
EC 1.6.2
NADPH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/NADPH%20dehydrogenase | In enzymology, a NADPH dehydrogenase () is an enzyme that catalyzes the chemical reaction
NADPH + H+ + acceptor NADP+ + reduced acceptor
The 3 substrates of this enzyme are NADPH, H+, and acceptor, whereas its two products are NADP+ and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. It has 2 cofactors: FAD, and FMN.
Nomenclature
The systematic name of this enzyme class is NADPH:acceptor oxidoreductase. Other names in common use include
NADPH2 diaphorase
NADPH diaphorase
old yellow enzyme
diaphorase
dihydronicotinamide adenine dinucleotide phosphate dehydrogenase
NADPH-dehydrogenase
NADPH-diaphorase
NADPH2-dehydrogenase
old yellow enzyme
reduced nicotinamide adenine dinucleotide phosphate dehydrogenase
TPNH dehydrogenase
TPNH-diaphorase
triphosphopyridine diaphorase
triphosphopyridine nucleotide diaphorase
NADPH2 dehydrogenase
NADPH:(acceptor) oxidoreductase.
References
Further reading
EC 1.6.99
NADPH-dependent enzymes
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/NAD%28P%29H%20dehydrogenase%20%28quinone%29 | In enzymology, a NAD(P)H dehydrogenase (quinone) () is an enzyme that catalyzes the chemical reaction
NAD(P)H + H+ + a quinone NAD(P)+ + a hydroquinone
The 4 substrates of this enzyme are NADH, NADPH, H+, and quinone, whereas its 3 products are NAD+, NADP+, and hydroquinone.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a quinone or similar compound as acceptor. The systematic name of this enzyme class is NAD(P)H:quinone oxidoreductase. Other names in common use include menadione reductase, phylloquinone reductase, quinone reductase, dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate,, quinone), DT-diaphorase, flavoprotein NAD(P)H-quinone reductase, menadione oxidoreductase, NAD(P)H dehydrogenase, NAD(P)H menadione reductase, NAD(P)H-quinone dehydrogenase, NAD(P)H-quinone oxidoreductase, NAD(P)H: (quinone-acceptor)oxidoreductase, NAD(P)H: menadione oxidoreductase, NADH-menadione reductase, naphthoquinone reductase, p-benzoquinone reductase, reduced NAD(P)H dehydrogenase, viologen accepting pyridine nucleotide oxidoreductase, vitamin K reductase, diaphorase, reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase, vitamin-K reductase, NAD(P)H2 dehydrogenase (quinone), NQO1, QR1, and NAD(P)H:(quinone-acceptor) oxidoreductase. This enzyme participates in biosynthesis of steroids. It employs one cofactor, FAD. At least one compound, Dicumarol is known to inhibit this enzyme.
Structural s |
https://en.wikipedia.org/wiki/NADPH%20dehydrogenase%20%28quinone%29 | In enzymology, a NADPH dehydrogenase (quinone) () is an enzyme that catalyzes the chemical reaction
NADPH + H+ + acceptor NADP+ + reduced acceptor
The 3 substrates of this enzyme are NADPH, H+, and acceptor, whereas its two products are NADP+ and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. The systematic name of this enzyme class is NADPH:(quinone-acceptor) oxidoreductase. Other names in common use include reduced nicotinamide adenine dinucleotide phosphate (quinone), dehydrogenase, NADPH oxidase, and NADPH2 dehydrogenase (quinone). It has 2 cofactors: FAD, and Flavoprotein. Several compounds are known to inhibit this enzyme, including Folate, and Dicumarol.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
See also
NdhF
References
EC 1.6.5
NADPH-dependent enzymes
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/CRYAB | Alpha-crystallin B chain is a protein that in humans is encoded by the CRYAB gene. It is part of the small heat shock protein family and functions as molecular chaperone that primarily binds misfolded proteins to prevent protein aggregation, as well as inhibit apoptosis and contribute to intracellular architecture. Post-translational modifications decrease the ability to chaperone. Mutations in CRYAB cause different cardiomyopathies, skeletal myopathies mainly myofibrillar myopathy, and also cataracts. In addition, defects in this gene/protein have been associated with cancer and neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.
Structure
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups.
Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic |
https://en.wikipedia.org/wiki/NADPH%E2%80%94hemoprotein%20reductase | In enzymology, a NADPH—hemoprotein reductase is an enzyme that catalyzes the chemical reaction
NADPH + H+ + n oxidized hemoprotein NADP+ + n reduced hemoprotein
The 3 substrates of this enzyme are NADPH, H+, and oxidized hemoprotein, whereas its two products are NADP+ and reduced hemoprotein. It has 2 cofactors: FAD, and FMN.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a heme protein as acceptor. The systematic name of this enzyme class is NADPH:hemoprotein oxidoreductase. Other names include cytochrome P450 reductase, ferrihemoprotein P-450 reductase, and NADPH-dependent cytochrome c reductase.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .
References
EC 1.6.2
NADPH-dependent enzymes
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/NADPH%3Aquinone%20reductase | In enzymology, a NADPH:quinone reductase () is an enzyme that catalyzes the chemical reaction
NADPH + H+ + 2quinone NADP+ + 2semiquinone
The 3 substrates of this enzyme are NADPH, H+, and quinone, whereas its two products are NADP+ and semiquinone.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a quinone or similar compound as acceptor. The systematic name of this enzyme class is NADPH:quinone oxidoreductase. This enzyme is also called NADPH2:quinone reductase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.6.5
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/NAD%28P%29%2B%20transhydrogenase%20%28Re/Si-specific%29 | {{DISPLAYTITLE:NAD(P)+ transhydrogenase (Re/Si-specific)}}
In enzymology, a NAD(P)+ transhydrogenase (Re/Si-specific () is an enzyme that catalyzes the chemical reaction
NADPH + NAD+ NADP+ + NADH
Thus, the two substrates of this enzyme are NADPH and NAD+, whereas its two products are NADP+ and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with NAD+ or NADP+ as acceptor. This enzyme participates in nicotinate and nicotinamide metabolism.
Nomenclature
The systematic name of this enzyme class is NADPH:NAD+ oxidoreductase (Re/Si-specific). Other names in common use include pyridine nucleotide transhydrogenase, transhydrogenase, NAD(P)+ transhydrogenase, nicotinamide adenine dinucleotide (phosphate) transhydrogenase, NAD+ transhydrogenase, NADH transhydrogenase, nicotinamide nucleotide transhydrogenase, NADPH-NAD+ transhydrogenase, pyridine nucleotide transferase, NADPH-NAD+ oxidoreductase, NADH-NADP+-transhydrogenase, NADPH:NAD+ transhydrogenase, H+-Thase, energy-linked transhydrogenase, and NAD(P)+ transhydrogenase (AB-specific).
References
Further reading
EC 1.6.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/NAD%28P%29%2B%20transhydrogenase%20%28Si-specific%29 | {{DISPLAYTITLE:NAD(P)+ transhydrogenase (Si-specific)}}
In biochemistry, NAD(P)+ transhydrogenase (Si-specific) () is an enzyme that catalyzes the chemical reaction
NADPH + NAD+ NADP+ + NADH
Thus, the two substrates of this enzyme are NADPH and NAD+, whereas its two products are NADP+ and NADH. This enzyme participates in nicotinate and nicotinamide metabolism. It employs one cofactor, FAD.
Physiological function
Si-specific transhydrogenase is a soluble protein found in some Gammaproteobacteria and gram-positive bacteria. Enterobacteriaceae are known to possess both a soluble and a membrane-bound transhydrogenase. In living cells this enzyme primarily operates in the direction consuming NADPH and producing NADH, as the physiological ratio of NADPH/NADP+ is much higher than the ratio of NADH/NAD+. Its chief function in vivo is the reoxidization of excess NADPH.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with NAD+ or NADP+ as acceptor. The systematic name of this enzyme is NADPH:NAD+ oxidoreductase (Si-specific). Other names in common use include non-energy-linked transhydrogenase, NAD(P)+ transhydrogenase (B-specific), and soluble transhydrogenase.
Older literature often uses ambiguous names such as pyridine nucleotide transhydrogenase, transhydrogenase, NAD(P)+ transhydrogenase, nicotinamide nucleotide transhydrogenase, NADPH-NAD+ transhydrogenase, pyridine nucleotide transferase, or NADPH-NAD+ o |
https://en.wikipedia.org/wiki/N-hydroxy-2-acetamidofluorene%20reductase | In enzymology, a N-hydroxy-2-acetamidofluorene reductase () is an enzyme that catalyzes the chemical reaction
2-acetamidofluorene + NAD(P)+ + H2O N-hydroxy-2-acetamidofluorene + NAD(P)H + H+
The 4 substrates of this enzyme are 2-acetamidofluorene, NAD+, NADP+, and H2O, whereas its 4 products are N-hydroxy-2-acetamidofluorene, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-acetamidofluorene:NAD(P)+ oxidoreductase. Other names in common use include N-hydroxy-2-acetylaminofluorene reductase, and NAD(P)H:N-hydroxy-2-acetamidofluorene N-oxidoreductase.
References
EC 1.7.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nicotine%20dehydrogenase | In enzymology, a nicotine dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-nicotine + acceptor + H2O (S)-6-hydroxynicotine + reduced acceptor
The 3 substrates of this enzyme are (S)-nicotine, acceptor, and H2O, whereas its two products are (S)-6-hydroxynicotine and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is nicotine:acceptor 6-oxidoreductase (hydroxylating). Other names in common use include nicotine oxidase, D-nicotine oxidase, nicotine:(acceptor) 6-oxidoreductase (hydroxylating), and L-nicotine oxidase. It has 2 cofactors: metal, and FMN.
References
EC 1.5.99
Metal enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nitric-oxide%20reductase | Nitric oxide reductase, an enzyme, catalyzes the reduction of nitric oxide (NO) to nitrous oxide (N2O). The enzyme participates in nitrogen metabolism and in the microbial defense against nitric oxide toxicity. The catalyzed reaction may be dependent on different participating small molecules: Cytochrome c (EC: 1.7.2.5, Nitric oxide reductase (cytochrome c)), NADPH (EC:1.7.1.14), or Menaquinone (EC:1.7.5.2).
Nomenclature
Nitric oxide reductase was assigned Enzyme Commission number (EC) 1.7.2.5. Enzyme Commission numbers are the standard naming system used for enzymes. The EC identifies the class, subclass, sub-subclass, and serial number of the enzyme. Nitric oxide reductase is in Class 1, therefore it is an oxidoreductases.
Nitric oxide reductase belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with other acceptors. The systematic name of this enzyme class is nitrous-oxide:acceptor oxidoreductase (NO-forming). Other names in common use include nitrogen oxide reductase, and nitrous-oxide:(acceptor) oxidoreductase (NO-forming).
Function
Organisms reduce nitrate (NO3−) to nitrogen gas (N2) through the process of denitrification, see Figure 1. Two important intermediates of the reduction pathway are nitric oxide (NO) and nitrous oxide (N2O). The reducing reaction that transforms NO into N2O is catalyzed by nitric oxide reductase (NOR).
NO is reduced to N2O also to prevent cellular toxicity. N2O, a potent gree |
https://en.wikipedia.org/wiki/Cytochrome%20c%20nitrite%20reductase | Cytochrome c nitrite reductase (ccNiR) () is a bacterial enzyme that catalyzes the six electron reduction of nitrite to ammonia; an important step in the biological nitrogen cycle. The enzyme catalyses the second step in the two step conversion of nitrate to ammonia, which allows certain bacteria to use nitrite as a terminal electron acceptor, rather than oxygen, during anaerobic conditions. During this process, ccNiR draws electrons from the quinol pool, which are ultimately provided by a dehydrogenase such as formate dehydrogenase or hydrogenase. These dehydrogenases are responsible for generating a proton motive force.
Cytochrome c Nitrite Reductase is a homodimer which contains five c-type heme cofactors per monomer. Four of the heme centers are bis-histidine ligated and presumably serve to shuttle electrons to the active site. The active site heme, however, is uniquely ligated by a single lysine residue.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is ammonia:ferricytochrome-c oxidoreductase.
References
Further reading
EC 1.7.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nitrite%20reductase%20%28NAD%28P%29H%29 | In enzymology, a nitrite reductase [NAD(P)H] () is an enzyme that catalyzes the chemical reaction
ammonium hydroxide + 3 NAD(P)+ + H2O nitrite + 3 NAD(P)H + 3 H+
The 4 substrates of this enzyme are ammonium hydroxide, NAD+, NADP+, and H2O, whereas its 4 products are nitrite, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is ammonium-hydroxide:NAD(P)+ oxidoreductase. Other names in common use include nitrite reductase (reduced nicotinamide adenine dinucleotide, (phosphate)), NADH-nitrite oxidoreductase, NADPH-nitrite reductase, assimilatory nitrite reductase, nitrite reductase [NAD(P)H2], and NAD(P)H2:nitrite oxidoreductase. This enzyme participates in nitrogen metabolism. It has 3 cofactors: FAD, Iron, and Siroheme.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.7.1
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Iron enzymes
Siroheme enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nitrite%20reductase%20%28NO-forming%29 | In enzymology, a nitrite reductase (NO-forming) () is an enzyme that catalyzes the chemical reaction
nitric oxide + H2O + ferricytochrome c ⇌ nitrite + ferrocytochrome c + 2 H+
The 3 substrates of this enzyme are nitric oxide, H2O, and ferricytochrome c, whereas its 3 products are nitrite, ferrocytochrome c, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is nitric-oxide:ferricytochrome-c oxidoreductase. Other names in common use include cd-cytochrome nitrite reductase, [nitrite reductase (cytochrome)] [misleading, see comments.], cytochrome c-551:O2, NO2+ oxidoreductase, cytochrome cd, cytochrome cd1, hydroxylamine (acceptor) reductase, methyl viologen-nitrite reductase, nitrite reductase (cytochrome, and NO-forming). This enzyme participates in nitrogen metabolism. It has 3 cofactors: FAD, Iron, and Copper.
Structural studies
As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , and .
References
EC 1.7.2
Flavoproteins
Iron enzymes
Copper enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nitroalkane%20oxidase | In enzymology, a nitroalkane oxidase () is an enzyme that catalyzes the chemical reaction
a nitroalkane + H2O + O2 an aldehyde or ketone + nitrite + H2O2
The 3 substrates of this enzyme are nitroalkane, H2O, and O2, whereas its 4 products are aldehyde, ketone, nitrite, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with oxygen as acceptor. The systematic name of this enzyme class is nitroalkane:oxygen oxidoreductase. Other names in common use include nitroethane oxidase, NAO, and nitroethane:oxygen oxidoreductase. This enzyme participates in nitrogen metabolism.
References
EC 1.7.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nitroquinoline-N-oxide%20reductase | In enzymology, a nitroquinoline-N-oxide reductase () is an enzyme that catalyzes the chemical reaction
4-(hydroxyamino)quinoline N-oxide + 2 NAD(P)+ + H2O 4-nitroquinoline N-oxide + 2 NAD(P)H + 2 H+
The 4 substrates of this enzyme are 4-hydroxyaminoquinoline N-oxide, NAD+, NADP+, and H2O, whereas its 4 products are 4-nitroquinoline N-oxide, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-(hydroxyamino)quinoline N-oxide:NADP+ oxidoreductase. Other names in common use include 4-nitroquinoline 1-oxide reductase, 4NQO reductase, and NAD(P)H2:4-nitroquinoline-N-oxide oxidoreductase.
References
EC 1.7.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nitrous-oxide%20reductase | In enzymology, a nitrous oxide reductase also known as nitrogen:acceptor oxidoreductase (N2O-forming) is an enzyme that catalyzes the final step in bacterial denitrification, the reduction of nitrous oxide to dinitrogen.
N2O + 2 reduced cytochome c N2 + H2O + 2 cytochrome c
It plays a critical role in preventing release of a potent greenhouse gas into the atmosphere.
Function
N2O is an inorganic metabolite of the prokaryotic cell during denitrification. Thus, denitrifiers comprise the principal group of N2O producers, with roles played also by nitrifiers, methanotrophic bacteria, and fungi. Among them, only denitrifying prokaryotes have the ability to convert N2O to N2. Conversion of N2O into N2 is the last step of a complete nitrate denitrification process and is an autonomous form of respiration. N2O is generated in the denitrifying cell by the activity of respiratory NO reductase. Some microbial communities have only capability of N2O reduction to N2 and does not have the other denitrification pathways such communities are known as nitrous oxide reducers. Some denitrifiers do not have complete denitrification with end product N2O
Structure
Nitrous-oxide reductase is a homodimer that is located in the bacterial periplasm. X-ray structures of the enzymes from Pseudomonas nautica and Paracoccus denitrificans have revealed that each subunit (MW=65 kDa) is organized into two domains. One cupredoxin-like domain contains a binuclear copper protein known as CuA.
The sec |
https://en.wikipedia.org/wiki/N-methylalanine%20dehydrogenase | In enzymology, a N-methylalanine dehydrogenase () is an enzyme that catalyzes the chemical reaction
N-methyl-L-alanine + H2O + NADP+ pyruvate + methylamine + NADPH + H+
The 3 substrates of this enzyme are N-methyl-L-alanine, H2O, and NADP+, whereas its 4 products are pyruvate, methylamine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N-methyl-L-alanine:NADP+ oxidoreductase (demethylating, deaminating).
References
EC 1.4.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/EIF4E | Eukaryotic translation initiation factor 4E, also known as eIF4E, is a protein that in humans is encoded by the EIF4E gene.
Structure and function
Most eukaryotic cellular mRNAs are blocked at their 5'-ends with the 7-methyl-guanosine five-prime cap structure, m7GpppX (where X is any nucleotide). This structure is involved in several cellular processes including enhanced translational efficiency, splicing, mRNA stability, and RNA nuclear export. eIF4E is a eukaryotic translation initiation factor involved in directing ribosomes to the cap structure of mRNAs as well as other steps in RNA metabolism that require cap-binding. It is a 24-kD polypeptide that exists as both a free form and as part of the eIF4F pre-initiation complex. Many cellular mRNAs require eIF4E in order to be translated into protein. The eIF4E polypeptide is considered by some to be the rate-limiting component of the eukaryotic translation apparatus and is involved in the mRNA-ribosome binding step of eukaryotic protein synthesis.
The other subunits of eIF4F are a 47-kD polypeptide, termed eIF4A, that possesses ATPase and RNA helicase activities, and a 220-kD scaffolding polypeptide, eIF4G.
Some viruses cut eIF4G in such a way that the eIF4E binding site is removed and the virus is able to translate its proteins without eIF4E. Also some cellular proteins, the most notable being heat shock proteins, do not require eIF4E in order to be translated. Both viruses and cellular proteins achieve this through an i |
https://en.wikipedia.org/wiki/N-methyl-L-amino-acid%20oxidase | In enzymology, a N-methyl-L-amino-acid oxidase () is an enzyme that catalyzes the chemical reaction
an N-methyl-L-amino acid + H2O + O2 an L-amino acid + formaldehyde + H2O2
The 3 substrates of this enzyme are N-methyl-L-amino acid, H2O, and O2, whereas its 3 products are L-amino acid, formaldehyde, and H2O2.
It has 2 cofactors: FAD, and Flavoprotein.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is N-methyl-L-amino-acid:oxygen oxidoreductase (demethylating). Other names in common use include N-methylamino acid oxidase, and demethylase.
References
Further reading
EC 1.5.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Opine%20dehydrogenase | In enzymology, an opine dehydrogenase () is an enzyme that catalyzes the chemical reaction
(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate + NAD+ + H2O L-2-aminopentanoic acid + pyruvate + NADH + H+
The 3 substrates of this enzyme are [[(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate]], NAD+, and H2O, whereas its 4 products are L-2-aminopentanoic acid, pyruvate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate:NAD+ oxidoreductase (L-aminopentanoate-forming). Other names in common use include (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+,, and L-aminopentanoate-forming).
References
EC 1.5.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/P-benzoquinone%20reductase%20%28NADPH%29 | In enzymology, a p-benzoquinone reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
NADPH + H+ + p-benzoquinone NADP+ + hydroquinone
The 3 substrates of this enzyme are NADPH, H+, and p-benzoquinone, whereas its two products are NADP+ and hydroquinone.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a quinone or similar compound as acceptor. The systematic name of this enzyme class is NADPH:p-benzoquinone oxidoreductase. This enzyme participates in gamma-hexachlorocyclohexane degradation.
References
EC 1.6.5
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Peptide-methionine%20%28R%29-S-oxide%20reductase | In enzymology, a peptide-methionine (R)-S-oxide reductase () is an enzyme that catalyzes the chemical reaction
peptide-L-methionine + thioredoxin disulfide + H2O peptide-L-methionine (R)-S-oxide + thioredoxin
The 3 substrates of this enzyme are peptide-L-methionine, thioredoxin disulfide, and H2O, whereas its two products are peptide-L-methionine (R)-S-oxide and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is peptide-methionine:thioredoxin-disulfide S-oxidoreductase [methionine (R)-S-oxide-forming]. Other names in common use include MsrB, methionine sulfoxide reductase (ambiguous), pMSR, methionine S-oxide reductase (ambiguous), selenoprotein R, methionine S-oxide reductase (R-form oxidizing), methionine sulfoxide reductase B, SelR, SelX, PilB, and pRMsr.
References
EC 1.8.4
Enzymes of unknown structure
Selenoproteins |
https://en.wikipedia.org/wiki/Phenylalanine%20dehydrogenase | In enzymology, a phenylalanine dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-phenylalanine + H2O + NAD+ phenylpyruvate + NH3 + NADH + H+
The 3 substrates of this enzyme are L-phenylalanine, H2O, and NAD+, whereas its 4 products are phenylpyruvate, NH3, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-phenylalanine:NAD+ oxidoreductase (deaminating). Other names in common use include L-phenylalanine dehydrogenase, and PHD. This enzyme participates in phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 1.4.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphoadenylyl-sulfate%20reductase%20%28thioredoxin%29 | In enzymology, a phosphoadenylyl-sulfate reductase (thioredoxin) () is an enzyme that catalyzes the chemical reaction
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide 3'-phosphoadenylyl sulfate + thioredoxin
The 3 substrates of this enzyme are adenosine 3',5'-bisphosphate, sulfite, and thioredoxin disulfide, whereas its two products are 3'-phosphoadenylyl sulfate and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is adenosine 3',5'-bisphosphate,sulfite:thioredoxin-disulfide oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming). Other names in common use include PAPS reductase, thioredoxin-dependent, PAPS reductase, thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase, 3'-phosphoadenylylsulfate reductase, thioredoxin:3'-phospho-adenylylsulfate reductase, phosphoadenosine-phosphosulfate reductase, adenosine 3',5'-bisphosphate,sulfite:oxidized-thioredoxin, and oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming). This enzyme participates in sulfur metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.8.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Polyamine%20oxidase | A polyamine oxidase (PAO) is an enzymatic flavoprotein that oxidizes a carbon-nitrogen bond in a secondary amino group of a polyamine donor, using molecular oxygen as an acceptor. The generalized PAO reaction converts three substrates (water, oxygen, and a polyamine with both primary and secondary amino groups) into three products (hydrogen peroxide, an amino-aldehyde, and a primary amine). Different PAOs with varying substrate specificities exist in different organisms. Phylogenetic analyses suggest that PAOs likely evolved once in eukaryotes and diversified by divergent evolution and gene duplication events, though some prokaryotes have acquired PAOs through horizontal gene transfer.
Structure and Mechanism
Structures of PAOs from corn, brewer's yeast, and mice contain a substrate-binding domain and an FAD-binding domain that secures the FAD cofactor non-covalently. The active site is located at the interface of these domains.
Active sites in PAOs vary, but some features are essential. The most strictly-conserved active site amino acid codons in PAO genes are a K residue at position 300 and an aromatic residue (F, Y, or H) at position 403 (numbers refer to homologous positions in the sequence of ZmPAO1, a PAO found in corn). K300 hydrogen-bonds to a water molecule, which also hydrogen-bonds to the catalytic N5 nitrogen atom of FAD. In corn, this complex modulates redox potential and reoxidation rate of the cofactor and may be involved in stabilizing the reduced cof |
https://en.wikipedia.org/wiki/Prenylcysteine%20oxidase | In enzymology, a prenylcysteine oxidase () is an enzyme that catalyzes the chemical reaction
an S-prenyl-L-cysteine + O2 + H2O a prenal + L-cysteine + H2O2
The 3 substrates of this enzyme are S-prenyl-L-cysteine, O2, and H2O, whereas its 3 products are prenal, L-cysteine, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is S-prenyl-L-cysteine:oxygen oxidoreductase. This enzyme is also called prenylcysteine lyase.
Human protein and gene
Prenylcysteine oxidase 1, symbol PCYOX1, gene on chromosome 2
See also
Hemithioacetals in nature, for mechanism of action
Flavin adenine dinucleotide, cofactor of the enzyme
Prenylation, a process forming S-prenyl-L-cysteine
References
EC 1.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/PreQ1%20synthase | In enzymology, a preQ1 synthase () is an enzyme that catalyzes the chemical reaction
7-aminomethyl-7-carbaguanine + 2 NADP+ 7-cyano-7-carbaguanine + 2 NADPH + 2 H+
Thus, the two substrates of this enzyme are 7-aminomethyl-7-carbaguanine and NADP+, whereas its 3 products are 7-cyano-7-carbaguanine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7-aminomethyl-7-carbaguanine:NADP+ oxidoreductase. Other names in common use include YkvM, QueF, preQ0 reductase, preQ0 oxidoreductase, 7-cyano-7-deazaguanine reductase, 7-aminomethyl-7-carbaguanine:NADP+ oxidoreductase, queuine synthase (incorrect as queuine is not the product), and queuine:NADP+ oxidoreductase (incorrect as queuine is not the product).
References
EC 1.7.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Proline%20dehydrogenase | In enzymology, proline dehydrogenase (PRODH) (EC 1.5.5.2, formerly EC 1.5.99.8) is an enzyme of the oxidoreductase family, active in the oxidation of L-proline to (S)-1-pyrroline-5-carboxylate during proline catabolism. The end product of this reaction is then further oxidized in a (S)-1-pyrroline-5-carboxylate dehydrogenase (P5CDH)-dependent reaction of the proline metabolism, or spent to produce ornithine, a crucial metabolite of ornithine and arginine metabolism. The systematic name of this enzyme class is L-proline:quinone oxidoreductase. Other names in common use include L-proline dehydrogenase, L-proline oxidase,and L-proline:(acceptor) oxidoreductase. It employs one cofactor, FAD, which requires riboflavin (vitamin B2).
Proline dehydrogenase is in humans encoded by PRODH and PRODH2 genes, located on the chromosomes 22 and 19, respectively. Their mutations lead to hyperprolinemia, manifested by increased proline levels in blood and urine. The deficiency of PRODH has also been linked to the susceptibility to schizophrenia-4.
Structure
The tertiary structure of PRODH consists of two interacting protein chains, connected by a mutual interaction between alpha helices of both chains. Each protein chain binds a separate FAD cofactor, necessary for the oxidative activity of the enzyme. The binding of FAD is mediated by electrostatic and non-polar interactions between the cofactor and twelve amino acid residues. In some bacteria, PRODH activity is exhibited in combination w |
https://en.wikipedia.org/wiki/Protein-disulfide%20reductase | In enzymology, a protein-disulfide reductase () is an enzyme that catalyzes the chemical reaction
protein dithiol + NAD(P)+ protein disulfide + NAD(P)H + H+
The 3 substrates of this enzyme are protein dithiol, NAD+, and NADP+, whereas its 4 products are protein disulfide, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is protein-dithiol:NAD(P)+ oxidoreductase. Other names in common use include protein disulphide reductase, insulin-glutathione transhydrogenase, disulfide reductase, and NAD(P)H2:protein-disulfide oxidoreductase.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 1.8.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Protein-disulfide%20reductase%20%28glutathione%29 | In enzymology, a protein-disulfide reductase (glutathione) () is an enzyme that catalyzes the chemical reaction
2 glutathione + protein-disulfide glutathione disulfide + protein-dithiol
Thus, the two substrates of this enzyme are glutathione and protein disulfide, whereas its two products are glutathione disulfide and protein dithiol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is glutathione:protein-disulfide oxidoreductase. Other names in common use include glutathione-insulin transhydrogenase, insulin reductase, reductase, protein disulfide (glutathione), protein disulfide transhydrogenase, glutathione-protein disulfide oxidoreductase, protein disulfide reductase (glutathione), GSH-insulin transhydrogenase, protein-disulfide interchange enzyme, protein-disulfide isomerase/oxidoreductase, thiol:protein-disulfide oxidoreductase, and thiol-protein disulphide oxidoreductase. This enzyme participates in glutathione metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.8.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Pteridine%20reductase | In enzymology, a pteridine reductase () is an enzyme that catalyzes the chemical reaction
5,6,7,8-tetrahydrobiopterin + 2 NADP+ biopterin + 2 NADPH + 2 H+
Thus, the two substrates of this enzyme are 5,6,7,8-tetrahydrobiopterin and NADP+, whereas its 3 products are biopterin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,6,7,8-tetrahydrobiopterin:NADP+ oxidoreductase. Other names in common use include PTR1, and pteridine reductase 1.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/HSP90AB1 | Heat shock protein HSP 90-beta also called HSP90beta is a protein that in humans is encoded by the HSP90AB1 gene.
Function
HSP90AB1 is a molecular chaperone. Chaperones are proteins that bind to other proteins, thereby stabilizing them in an ATP-dependent manner. Chaperones stabilize new proteins during translation, mature proteins which are partially unstable but also proteins that have become partially denatured due to various kinds of cellular stress. In case proper folding or refolding is impossible, HSPs mediate protein degradation. They also have specialized functions, such as intracellular transport into organelles.
Classification
Human HSPs are classified into 5 major groups according to the HGNC:
HSP70
DnaJ (HSP40)
HSPB (small heat shock proteins)
HSPC (HSP90)
chaperonins
Chaperonins are characterized by their barrel-shaped structure with binding sites for client proteins inside the barrels.
The human HSP90 group consists of 5 members according to the HGNC:
HSP90AA1 (heat shock protein 90 kDa alpha, class A, member 1)
HSP90AA3P (heat shock protein 90 alpha family class A member 3, pseudogene)
HSP90AB1 (heat shock protein 90 kDa alpha, class B, member 1) (this protein)
HSP90B1 (heat shock protein 90 kDA beta, member 1)
TRAP1 (TNF receptor associated protein 1)
Whereas HSP90AA1 and HSP90AB1 are located primarily in the cytoplasm of the cells, HSP90B1 can be found in the endoplasmic reticulum and Trap1 in mitochondria.
Co-chaperones
Co-chaperones bind |
https://en.wikipedia.org/wiki/Putrescine%20oxidase | In enzymology, a putrescine oxidase () is an enzyme that catalyzes the chemical reaction
putrescine + O2 + H2O 4-aminobutanal + NH3 + H2O2
The 3 substrates of this enzyme are putrescine, O2, and H2O, whereas its 3 products are 4-aminobutanal, NH3, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is putrescine:oxygen oxidoreductase (deaminating). This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, FAD.
References
EC 1.4.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyrimidodiazepine%20synthase | In enzymology, a pyrimidodiazepine synthase () is an enzyme that catalyzes the chemical reaction
a pyrimidodiazepine + glutathione disulfide + H2O 6-pyruvoyltetrahydropterin + 2 glutathione
The 3 substrates of this enzyme are pyrimidodiazepine, glutathione disulfide, and H2O, whereas its two products are 6-pyruvoyltetrahydropterin and glutathione.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with a disulfide as acceptor. The systematic name of this enzyme class is pyrimidodiazepine:glutathione-disulfide oxidoreductase (ring-opening, cyclizing). Other names in common use include PDA synthase, pyrimidodiazepine:oxidized-glutathione oxidoreductase (ring-opening,, and cyclizing). This enzyme participates in glutathione metabolism.
References
EC 1.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/ICAM2 | Intercellular adhesion molecule 2 (ICAM2), also known as CD102 (Cluster of Differentiation 102), is a human gene, and the protein resulting from it.
Protein structure
The protein encoded by this gene is a member of the intercellular adhesion molecule (ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 2–9 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein.
Protein functions
ICAM-2 molecules regulate spermatid adhesion on Sertoli cell on the apical side of the blood-testis barrier (towards the lumen), thus playing a major role in spermatogenesis.
This protein may also play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance.
Interactions
ICAM2 has been shown to interact with EZR. It has also been shown to bind to P9 (Uniprot: B2UM07), a secreted protein from Akkermansia muciniphila.
See also
Cluster of differentiation
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Intercellular adhesion molecule 2 (ICAM2)
Clusters of differentiation |
https://en.wikipedia.org/wiki/Pyrroline-2-carboxylate%20reductase | In enzymology, a pyrroline-2-carboxylate reductase () is an enzyme that catalyzes the chemical reaction
L-proline + NAD(P)+ 1-pyrroline-2-carboxylate + NAD(P)H + H+
The 3 substrates of this enzyme are L-proline, NAD+, and NADP+, whereas its 4 products are 1-pyrroline-2-carboxylate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-proline:NAD(P)+ 2-oxidoreductase. This enzyme is also called Delta1-pyrroline-2-carboxylate reductase. This enzyme participates in lysine degradation and arginine and proline metabolism.
References
EC 1.5.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyrroline-5-carboxylate%20reductase | In enzymology, a pyrroline-5-carboxylate reductase () is an enzyme that catalyzes the chemical reaction
L-proline + NAD(P)+ 1-pyrroline-5-carboxylate + NAD(P)H + H+
The 3 substrates of this enzyme are L-proline, NAD+, and NADP+, whereas its 4 products are 1-pyrroline-5-carboxylate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-proline:NAD(P)+ 5-oxidoreductase. Other names in common use include proline oxidase, L-proline oxidase, 1-pyrroline-5-carboxylate reductase, NADPH-L-Delta1-pyrroline carboxylic acid reductase, and L-proline-NAD(P)+ 5-oxidoreductase. This enzyme participates in arginine and proline metabolism.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
Human genes
PYCR1, nuclear gene for mitochondrial protein
PYCR2, nuclear gene for mitochondrial protein
PYCR3 (formerly PYCRL), cytosolic protein
References
EC 1.5.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28R%29-6-hydroxynicotine%20oxidase | In enzymology, a (R)-6-hydroxynicotine oxidase () is an enzyme that catalyzes the chemical reaction
(R)-6-hydroxynicotine + HO + O 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + HO
The 3 substrates of this enzyme are (R)-6-hydroxynicotine, HO, and O, whereas its two products are 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is (R)-6-hydroxynicotine:oxygen oxidoreductase. Other names in common use include D-6-hydroxynicotine oxidase, and 6-hydroxy-D-nicotine oxidase. 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 1.5.3
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28S%29-6-hydroxynicotine%20oxidase | In enzymology, a (S)-6-hydroxynicotine oxidase () is an enzyme that catalyzes the chemical reaction
(S)-6-hydroxynicotine + HO + O 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + HO
The 3 substrates of this enzyme are (S)-6-hydroxynicotine, HO, and O, whereas its two products are 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one and HO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is (S)-6-hydroxynicotine:oxygen oxidoreductase. Other names in common use include L-6-hydroxynicotine oxidase, 6-hydroxy-L-nicotine oxidase, and 6-hydroxy-L-nicotine:oxygen oxidoreductase. It employs one cofactor, FAD.
References
EC 1.5.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/MT-ND3 | MT-ND3 is a gene of the mitochondrial genome coding for the NADH dehydrogenase 3 (ND3) protein. The ND3 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Variants of MT-ND3 are associated with Mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS), Leigh's syndrome (LS) and Leber's hereditary optic neuropathy (LHON).
Structure
General features
MT-ND3 is located in human mitochondrial DNA from base pair 10,059 to 10,404. The MT-ND3 gene produces a 13 kDa protein composed of 115 amino acids. MT-ND3 is one of seven mitochondrial genes encoding subunits of the enzyme NADH dehydrogenase (ubiquinone), together with MT-ND1, MT-ND2, MT-ND4, MT-ND4L, MT-ND5, and MT-ND6. Also known as Complex I, this enzyme is the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centres and the NADH binding site. The MT-ND3 product and the rest of the mitochondrially encoded subunits are the most hydrophobic of the subunits of Complex I and form the core of the transmembrane region.
Untranslated extra nucleotide
In the MT-ND3 gene from many species of birds and turtles there is an extra nucleotide that is not translated to protein.
Translational frameshifting or RNA editing are alternative explan |
https://en.wikipedia.org/wiki/Saccharopine%20dehydrogenase%20%28NAD%2B%2C%20L-glutamate-forming%29 | In enzymology, a saccharopine dehydrogenase (NAD+, L-glutamate-forming) () is an enzyme that catalyzes the chemical reaction
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
The 3 substrates of this enzyme are N6-(L-1,3-dicarboxypropyl)-L-lysine, NAD+, and H2O, whereas its 4 products are L-glutamate, 2-aminoadipate 6-semialdehyde, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming). Other names in common use include dehydrogenase, saccharopine (nicotinamide adenine dinucleotide,, glutamate-forming), saccharopin dehydrogenase, NAD+ oxidoreductase (L-2-aminoadipic-delta-semialdehyde and, glutamate forming), aminoadipic semialdehyde synthase, saccharopine dehydrogenase (NAD+, L-glutamate-forming), 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase, and (L-glutamate-forming). This enzyme participates in lysine degradation.
References
EC 1.5.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Saccharopine%20dehydrogenase%20%28NAD%2B%2C%20L-lysine-forming%29 | In enzymology, a saccharopine dehydrogenase (NAD+, L-lysine-forming) () is an enzyme that catalyzes the chemical reaction
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O L-lysine + 2-oxoglutarate + NADH + H+
The 3 substrates of this enzyme are N6-(L-1,3-dicarboxypropyl)-L-lysine, NAD+, and H2O, whereas its 4 products are L-lysine, 2-oxoglutarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-lysine-forming). Other names in common use include lysine-2-oxoglutarate reductase, dehydrogenase, saccharopine (nicotinamide adenine dinucleotide,, lysine forming), epsilon-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine, forming), N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming), 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase, and (L-lysine-forming). This enzyme participates in lysine biosynthesis and lysine degradation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.5.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Saccharopine%20dehydrogenase%20%28NADP%2B%2C%20L-glutamate-forming%29 | In enzymology, a saccharopine dehydrogenase (NADP+, L-glutamate-forming) () is an enzyme that catalyzes the chemical reaction
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O L-glutamate + L-2-aminoadipate 6-semialdehyde + NADPH + H+
The 3 substrates of this enzyme are N6-(L-1,3-dicarboxypropyl)-L-lysine, NADP+, and H2O, whereas its 4 products are L-glutamate, L-2-aminoadipate 6-semialdehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming). Other names in common use include saccharopine (nicotinamide adenine dinucleotide phosphate,, glutamate-forming) dehydrogenase, aminoadipic semialdehyde-glutamic reductase, aminoadipate semialdehyde-glutamate reductase, aminoadipic semialdehyde-glutamate reductase, epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase, (L-2-aminoadipate-semialdehyde forming), saccharopine reductase, 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase, and (L-glutamate-forming). This enzyme participates in lysine biosynthesis and lysine degradation.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Notch%202 | Neurogenic locus notch homolog protein 2 (Notch 2) is a protein that in humans is encoded by the NOTCH2 gene.
NOTCH2 is associated with Alagille syndrome and Hajdu–Cheney syndrome.
Function
Notch 2 is a member of the notch family. Members of this Type 1 transmembrane protein family share structural characteristics including an extracellular domain consisting of multiple epidermal growth factor-like (EGF) repeats, and an intracellular domain consisting of multiple, different domain types. Notch family members play a role in a variety of developmental processes by controlling cell fate decisions. The Notch signaling network is an evolutionarily conserved intercellular signaling pathway that regulates interactions between physically adjacent cells. In Drosophila, notch interaction with its cell-bound ligands (delta, serrate) establishes an intercellular signaling pathway that plays a key role in development. Homologues of the notch-ligands have also been identified in human, but precise interactions between these ligands and the human notch homologues remain to be determined. This protein is cleaved in the trans-Golgi network, and presented on the cell surface as a heterodimer. This protein functions as a receptor for membrane bound ligands, and may play a role in vascular, renal and hepatic development.
Mutations within the last coding exon of Notch2 that remove the PEST domain and escape the nonsense-mediated mRNA decay have been shown to be the main cause of the Hajdu-Ch |
https://en.wikipedia.org/wiki/Ehrenpreis | Ehrenpreis is a surname. Notable people with the surname include:
Leon Ehrenpreis (1930–2010), American mathematician
Ehrenpreis conjecture
Malgrange–Ehrenpreis theorem
Mordecai Ehrenpreis, (1869–1951), Polish-Swedish rabbi
See also
Veronica (plant), German name: Ehrenpreis
German-language surnames |
https://en.wikipedia.org/wiki/Saccharopine%20dehydrogenase%20%28NADP%2B%2C%20L-lysine-forming%29 | In enzymology, a saccharopine dehydrogenase (NADP+, L-lysine-forming) () is an enzyme that catalyzes the chemical reaction
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O L-lysine + 2-oxoglutarate + NADPH + H+
The 3 substrates of this enzyme are N6-(L-1,3-dicarboxypropyl)-L-lysine, NADP+, and H2O, whereas its 4 products are L-lysine, 2-oxoglutarate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming). Other names in common use include lysine-2-oxoglutarate reductase, lysine-ketoglutarate reductase, L-lysine-alpha-ketoglutarate reductase, lysine:alpha-ketoglutarate:TPNH oxidoreductase, (epsilon-N-[gultaryl-2]-L-lysine forming), saccharopine (nicotinamide adenine dinucleotide phosphate,, lysine-forming) dehydrogenase, 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase, and (L-lysine-forming). This enzyme participates in lysine biosynthesis and lysine degradation.
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulfiredoxin | In enzymology, a sulfiredoxin () is an enzyme that catalyzes the chemical reaction
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
The 3 substrates of this enzyme are peroxiredoxin-(S-hydroxy-S-oxocysteine), ATP, and a thiol, whereas its 4 products are peroxiredoxin-(S-hydroxycysteine), ADP, phosphate, and a disulfide.
This enzyme is involved in antioxidant metabolism by re-activating peroxiredoxins, which are a group of peroxidases, when these enzymes are inhibited by over-oxidation.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other, known, acceptors. The systematic name of this enzyme class is peroxiredoxin-(S-hydroxy-S-oxocysteine):thiol oxidoreductase [ATP-hydrolysing; peroxiredoxin-(S-hydroxycysteine)-forming]. Other names in common use include Srx1, sulphiredoxin, and peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase.
Function
The sulfur atom in the side-chain of the amino acid cysteine can exist in several different oxidation states. The most reduced of these is as a thiol group (Cys-SH). Oxidation of cysteine produces cystine, which is one half of a disulfide bond (Cys-S-S-Cys). These lower oxidation states of cysteine (disulfides) are readily reversible, but higher oxidation states, such as sulfinic acid (Cys-SOOH), were once considered irreversible, biologically speaking. This view changed with the discovery of sulfiredoxin |
https://en.wikipedia.org/wiki/Sulfite%20reductase | Sulfite reductases () are enzymes that participate in sulfur metabolism. They catalyze the reduction of sulfite to hydrogen sulfide and water. Electrons for the reaction are provided by a dissociable molecule of either NADPH, bound flavins, or ferredoxins.
SO32− (sulfite) + electron donor H2S (hydrogen sulfide) + oxidized donor + 3 H2O
Sulfite reductases, which belong to the oxidoreductase family, are found in archaea, bacteria, fungi, and plants. They are grouped as either assimilatory or dissimilatory sulfite reductases depending on their function, their spectroscopic properties, and their catalytic properties. This enzyme participates in selenoamino acid metabolism and sulfur assimilation. It employs two covalently coupled cofactors - an iron sulfur cluster and a siroheme - which deliver electrons to the substrate via this coupling.
The systematic name of this enzyme class is hydrogen-sulfide:acceptor oxidoreductase. Other names in common use include assimilatory sulfite reductase, assimilatory-type sulfite reductase, and hydrogen-sulfide:(acceptor) oxidoreductase.
References
Further reading
EC 1.8.99
Iron enzymes
Sulfur metabolism |
https://en.wikipedia.org/wiki/Prostaglandin%20EP4%20receptor | {{DISPLAYTITLE:Prostaglandin EP4 receptor}}
Prostaglandin E2 receptor 4 (EP4) is a prostaglandin receptor for prostaglandin E2 (PGE2) encoded by the PTGER4 gene in humans; it is one of four identified EP receptors, the others being EP1, EP2, and EP3, all of which bind with and mediate cellular responses to PGE2 and also, but generally with lesser affinity and responsiveness, certain other prostanoids (see Prostaglandin receptors). EP4 has been implicated in various physiological and pathological responses in animal models and humans.
Gene
The PTGER4 gene is located on human chromosome 5p13.1 at position p13.1 (i.e. 5p13.1), contains 7 exons, and codes for a G protein-coupled receptor (GPCR) of the rhodopsin-like receptor family, Subfamily A14 (see rhodopsin-like receptors#Subfamily A14).
Expression
In humans, mRNA for EP4 has been detected by Northern blotting in the heart and small intestine and to lesser extents in lung, kidney, thymus, uterus, dorsal root ganglions, and brain. EP4 protein is found in humans as measured by immunochemistry in pulmonary veins; kidney glomeruli and Tunica media of kidney arteries; corpus cavernosum of the penis; carotid artery atherosclerotic plaques; Abdominal aorta aneurysms; corneal endothelium, corneal keratocytes, trabecular cells, ciliary epithelium, conjunctival stromal cells, and iridal stromal cells of the eye; and gingival fibroblasts.
Ligands
Activating ligands
Standard prostanoids have the following relative efficacies in bi |
https://en.wikipedia.org/wiki/PURA | Pur-alpha is a protein that in humans is encoded by the PURA gene located at chromosome 5, band q31.
Pur-alpha is an ancient, multi-functional DNA- and RNA-binding protein. PURA is expressed in every human tissue, where it exists as a protein of 322 amino acids. According to convention, PURA, the gene, is written italicized in all upper case letters. Pur-alpha, the protein, is written with the first letter capitalized and can be found listed as Pur-alpha, Pur-α, Pura, Puralpha, Pur alpha and Pur1.
Evolutionary conservation and function
Pur-alpha was the first sequence-specific single-stranded DNA-binding protein to be discovered in higher organisms (GenBank M96684.1; GI:190749). It binds to both single-stranded and double-stranded DNA, making contact with G residues in the purine-rich strand of its binding site. Cumulative data shows that Pur-alpha preferentially binds to the sequence (G2-4N1-3)n, where N is not G. N denotes a nucleotide, and n denotes the number of repeats of this small sequence. N may be repeated up to three times in this sequence. Following the identification of a Pur factor, which specifically bound a purine-rich sequence in the control region of the c-MYC gene, the gene, PURA, encoding the protein, Pur-alpha, was cloned and sequenced for both human and mouse (GenBank U02098.1). Pur-alpha belongs to the four-member Pur protein family, which also includes Pur-beta (GenBank AY039216.1; GI:14906267) and two forms of Pur–gamma (Variant A, GenBank AF19551 |
https://en.wikipedia.org/wiki/Taurine%20dehydrogenase | In enzymology, a taurine dehydrogenase () is an enzyme that catalyzes the chemical reaction.
taurine + H2O + acceptor sulfoacetaldehyde + NH3 + reduced acceptor
The 3 substrates of this enzyme are taurine, H2O, and acceptor, whereas its 3 products are sulfoacetaldehyde, NH3, and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with other acceptors. The systematic name of this enzyme class is taurine:acceptor oxidoreductase (deaminating). This enzyme is also called taurine:(acceptor) oxidoreductase (deaminating). This enzyme participates in nitrogen metabolism.
References
EC 1.4.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tauropine%20dehydrogenase | In enzymology, a tauropine dehydrogenase () is an enzyme that catalyzes the chemical reaction
tauropine + NAD+ + H2O taurine + pyruvate + NADH + H+
The 3 products of this enzyme are tauropine, NAD+, and H2O, whereas its 4 substrates are taurine, pyruvate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N2-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming). This enzyme is also called 2-N-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming).
References
EC 1.5.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiol%20oxidase | In enzymology, a thiol oxidase () is an enzyme that catalyzes the chemical reaction
4 R'C(R)SH + O2 2 R'C(R)S-S(R)CR' + 2 H2O
Thus, the two substrates of this enzyme are R'C(R)SH and O2, whereas its two products are R'C(R)S-S(R)CR' and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is thiol:oxygen oxidoreductase. This enzyme is also called sulfhydryl oxidase.
References
EC 1.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/RAD17 | Cell cycle checkpoint protein RAD17 is a protein that in humans is encoded by the RAD17 gene.
Function
The protein encoded by this gene is highly similar to the gene product of Schizosaccharomyces pombe rad17, a cell cycle checkpoint gene required for cell cycle arrest and DNA damage repair in response to DNA damage. This protein shares strong similarity with DNA replication factor C (RFC), and can form a complex with RFCs. This protein binds to chromatin prior to DNA damage and is phosphorylated by ATR after the damage. This protein recruits the RAD1-RAD9-HUS1 checkpoint protein complex onto chromatin after DNA damage, which may be required for its phosphorylation. The phosphorylation of this protein is required for the DNA-damage-induced cell cycle G2 arrest, and is thought to be a critical early event during checkpoint signaling in DNA-damaged cells. Eight alternatively spliced transcript variants of this gene, which encode four distinct proteins, have been reported.
Meiosis
During meiosis in yeast and in mammals, RAD17 protein functions as a DNA damage sensor promoting DNA checkpoint control. In yeast, the RAD17 protein facilitates proper assembly of the meiotic crossover recombination complex containing the RAD51 protein, thus promoting efficient repair of meiotic DNA double-strand breaks. During male meiosis in maize (Zea mays), the ZmRAD17 gene is involved in repair of DNA double strand breaks, likely by promoting synaptonemal complex assembly.
Interactions
RA |
https://en.wikipedia.org/wiki/Thiomorpholine-carboxylate%20dehydrogenase | In enzymology, a thiomorpholine-carboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
thiomorpholine 3-carboxylate + NAD(P)+ 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
The 3 substrates of this enzyme are thiomorpholine 3-carboxylate, NAD+, and NADP+, whereas its 4 products are 3,4-dehydro-thiomorpholine-3-carboxylate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is thiomorpholine-3-carboxylate:NAD(P)+ 5,6-oxidoreductase. Other names in common use include ketimine reductase, and ketimine-reducing enzyme.
CRYM, a taxon-specific crystallin protein that also binds thyroid hormones has thiomorpholine-carboxylate dehydrogenase activity.
References
EC 1.5.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/RAP1GAP | Rap1 GTPase-activating protein 1 is an enzyme that in humans is encoded by the RAP1GAP gene.
Interactions
RAP1GAP has been shown to interact with MLLT4.
References
Further reading |
https://en.wikipedia.org/wiki/Thiosulfate%20dehydrogenase | Thiosulfate dehydrogenase (abbreviated as TsdA) () is an enzyme that catalyzes the chemical reaction:
2 thiosulfate + 2 ferricytochrome c tetrathionate + 2 ferrocytochrome c
Thus, the two substrates of this enzyme are thiosulfate and ferricytochrome c, whereas its two products are tetrathionate and ferrocytochrome c.
Thiosulfate dehydrogenase homologues have been isolated from numerous bacterial species and differ slightly in structure but have analogous function and mechanism of sulfur oxidation. The enzyme is similar in both function and structure to a few enzymes in the Sox sulfur oxidation pathway.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a cytochrome as acceptor. The systematic name of this enzyme class is thiosulfate:ferricytochrome-c oxidoreductase. Other names in common use include tetrathionate synthase, thiosulfate oxidase, thiosulfate-oxidizing enzyme, and thiosulfate-acceptor oxidoreductase.
Structure
Thiosulfate dehydrogenase, isolated from the appreciably studied bacterial strain Allochromatium vinosum (253 peptide chain length, 25.8 kDa) is composed of two catalytic domains, each similar to cytochrome c, linked by a long unstructured peptide chain. The N-terminal domain is structurally homologous to the SoxA family of cytochrome enzymes while the C-terminal domain is representative of the standard mitochondrial cytochrome c family fold with high similarity to nitrite r |
https://en.wikipedia.org/wiki/Thiosulfate%20dehydrogenase%20%28quinone%29 | In enzymology, a thiosulfate dehydrogenase (quinone) () is an enzyme that catalyzes the chemical reaction
2 thiosulfate + 2 6-decylubiquinone tetrathionate + 2 6-decylubiquinol
Thus, the two substrates of this enzyme are thiosulfate and 6-decylubiquinone, whereas its two products are tetrathionate and 6-decylubiquinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a quinone or similar compound as acceptor. The systematic name of this enzyme class is thiosulfate:6-decylubiquinone oxidoreductase. Other names in common use include thiosulfate:quinone oxidoreductase, thiosulphate:quinone oxidoreductase, thiosulfate oxidoreductase, tetrathionate-forming, and TQO.
References
EC 1.8.5
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trimethylamine%20dehydrogenase | In enzymology, a trimethylamine dehydrogenase () is an enzyme that catalyzes the chemical reaction
trimethylamine + H2O + electron-transferring flavoprotein dimethylamine + formaldehyde + reduced electron-transferring flavoprotein
The 3 substrates of this enzyme are trimethylamine, H2O, and electron-transferring flavoprotein, whereas its 3 products are dimethylamine, formaldehyde, and reduced electron-transferring flavoprotein.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with a flavin as acceptor. The systematic name of this enzyme class is trimethylamine:electron-transferring flavoprotein oxidoreductase (demethylating). This enzyme participates in methane metabolism.
References
EC 1.5.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trimethylamine-N-oxide%20reductase%20%28cytochrome%20c%29 | In enzymology, a trimethylamine-N-oxide reductase (cytochrome c) () is an enzyme that catalyzes the chemical reaction
trimethylamine + 2 (ferricytochrome c)-subunit + H2O trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
The 3 substrates of this enzyme are trimethylamine, (ferricytochrome c)-subunit, and H2O, whereas its 3 products are trimethylamine N-oxide, (ferrocytochrome c)-subunit, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is trimethylamine:cytochrome c oxidoreductase. Other names in common use include TMAO reductase, and TOR. This enzyme participates in two-component system - general.
References
EC 1.7.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trypanothione-disulfide%20reductase | In enzymology, a trypanothione-disulfide reductase () is an enzyme that catalyzes the chemical reaction
trypanothione + NADP+ trypanothione disulfide + NADPH + H+
Thus, the two substrates of this enzyme are trypanothione and NADP+, whereas its 3 products are trypanothione disulfide, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is trypanothione:NADP+ oxidoreductase. Other names in common use include trypanothione reductase, and NADPH2:trypanothione oxidoreductase. It employs one cofactor, FAD.
The X-ray crystal structures of trypanothione reductase enzymes from several trypanosomatids species have been solved, including those from Crithidia fasciculata, Leishmania infantum, Trypanosoma brucei and Trypanosoma cruzi. The structures reveal that trypanothione reductase forms homodimers in solution with each of the two individual subunits comprising an FAD-binding domain, an NADPH-binding domain and an interface domain. Examples of trypanothione reductase inhibitors include 5-Nitro-Imidazole, Febrifugine, Imipramine and Benzoxaborole.
References
EC 1.8.1
NADPH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/BUB1B | Mitotic checkpoint serine/threonine-protein kinase BUB1 beta is an enzyme that in humans is encoded by the BUB1B gene. Also known as BubR1, this protein is recognized for its mitotic roles in the spindle assembly checkpoint (SAC) and kinetochore-microtubule interactions that facilitate chromosome migration and alignment. BubR1 promotes mitotic fidelity and protects against aneuploidy by ensuring proper chromosome segregation between daughter cells. BubR1 is proposed to prevent tumorigenesis.
Function
This gene encodes a kinase involved in spindle checkpoint function and chromosome segregation. The protein has been localized to the kinetochore and plays a role in the inhibition of the anaphase-promoting complex/cyclosome (APC/C), delaying the onset of anaphase and ensuring proper chromosome segregation. Impaired spindle checkpoint function has been found in many forms of cancer.
Increased expression of BubR1 in mice extends a healthy lifespan.
Clinical Significance
BubR1 has been implicated in a variety of biological processes and pathologies, including cancer, aging, mosaic variegated aneuploidy (MVA), and heart disease. BubR1 protein levels are shown to decline with age. Furthermore, loss of BubR1 in young organisms is associated with rapid aging and premature onset of age-related diseases and phenotypes such as cardiac dysfunction, poor wound healing, cataracts, kyphosis, fat loss and muscle wasting (cachexia), and cancer. This has been demonstrated in mice.
DNA repa |
https://en.wikipedia.org/wiki/Tryptophan%20dehydrogenase | In enzymology, a tryptophan dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-tryptophan + NAD(P)+ + H2O (indol-3-yl)pyruvate + NH3 + NAD(P)H + H+
The 4 substrates of this enzyme are L-tryptophan, NAD+, NADP+, and H2O, whereas its 5 products are (indol-3-yl)pyruvate, NH3, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-tryptophan:NAD(P)+ oxidoreductase (deaminating). Other names in common use include NAD(P)+-L-tryptophan dehydrogenase, L-tryptophan dehydrogenase, L-Trp-dehydrogenase, and TDH. This enzyme has at least one effector, calcium.
References
EC 1.4.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Valine%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Valine dehydrogenase (NADP+)}}
In enzymology, a valine dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
L-valine + H2O + NADP+ 3-methyl-2-oxobutanoate + NH3 + NADPH + H+
The 3 substrates of this enzyme are L-valine, H2O, and NADP+, whereas its 4 products are 3-methyl-2-oxobutanoate, NH3, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-valine:NADP+ oxidoreductase (deaminating). Other names in common use include valine dehydrogenase (nicotinamide adenine dinucleotide phosphate), and valine dehydrogenase (NADP+).
References
EC 1.4.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DNM2 | Dynamin-2 is a protein that in humans is encoded by the DNM2 gene.
Function
Dynamins represent one of the subfamilies of GTP-binding proteins. These proteins share considerable sequence similarity over the N-terminal portion of the molecule, which contains the GTPase domain. Dynamins are associated with microtubules. They have been implicated in cell processes such as endocytosis and cell motility, and in alterations of the membrane that accompany certain activities such as bone resorption by osteoclasts. Dynamins bind many proteins that bind actin and other cytoskeletal proteins. Dynamins can also self-assemble, a process that stimulates GTPase activity. Four alternatively spliced transcripts encoding different proteins have been described. Additional alternatively spliced transcripts may exist, but their full-length nature has not been determined.
Interactions
DNM2 has been shown to interact with:
SHANK1,
SHANK2, and
SNX9.
Clinical relevance
Mutations in this gene have been associated to cases of acute lymphoblastic leukaemia,
or congenital myopathy (centronuclear type).
References
Further reading
External links
GeneReviews/NIH/NCBI/UW entry on DNM2-Related Intermediate Charcot-Marie-Tooth Neuropathy or AD Charcot-Marie-Tooth Disease Type 2B
HGNC Approved Gene Symbol: DNM2, Cytogenetic location: 19p13.2,Genomic coordinates (GRCh38): 19:10,718,052-10,831,909 (from NCBI) |
https://en.wikipedia.org/wiki/Vomilenine%20reductase | In enzymology, a vomilenine reductase () is an enzyme that catalyzes the chemical reaction
1,2-dihydrovomilenine + NADP+ vomilenine + NADPH + H+
Thus, the two substrates of this enzyme are 1,2-dihydrovomilenine and NADP+, whereas its 3 products are vomilenine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1,2-dihydrovomilenine:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/60S%20ribosomal%20protein%20L5 | 60S ribosomal protein L5 is a protein that in humans is encoded by the RPL5 gene.
Function
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L18P family of ribosomal proteins. It is located in the cytoplasm. The protein binds 5S rRNA to form a stable complex called the 5S ribonucleoprotein particle (RNP), which is necessary for the transport of nonribosome-associated cytoplasmic 5S rRNA to the nucleolus for assembly into ribosomes. The protein interacts specifically with the beta subunit of casein kinase 2.
Clinical significance
Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found. This gene is co-transcribed with the small nucleolar RNA gene U21, which is located in its fifth intron. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
Interactions
Ribosomal protein L5 has been shown to interact with:
CSNK2B,
EIF5A,
Mdm2, and
PDCD4.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Diamond–Blackfan Anemia
OMIM entrie |
https://en.wikipedia.org/wiki/Fluid%20Concepts%20and%20Creative%20Analogies | Fluid Concepts and Creative Analogies: Computer Models of the Fundamental Mechanisms of Thought is a 1995 book by Douglas Hofstadter and other members of the Fluid Analogies Research Group exploring the mechanisms of intelligence through computer modeling. It contends that the notions of analogy and fluidity are fundamental to explain how the human mind solves problems and to create computer programs that show intelligent behavior. It analyzes several computer programs that members of the group have created over the years to solve problems that require intelligence.
It was the first book ever sold by Amazon.com.
Origin of the book
The book is a collection of revised articles that appeared in precedence, each preceded by an introduction by Hofstadter.
They describe the scientific work by him and his collaborators in the 1980s and 1990s.
The project started in the late 1970s at Indiana University.
In 1983 he took a sabbatical year at MIT, working in Marvin Minsky's Artificial Intelligence Lab.
There he met and collaborated with Melanie Mitchell, who then became his doctoral student.
Subsequently, Hofstadter moved to the University of Michigan, where the FARG (Fluid Analogies Research Group) was founded.
Eventually he returned to Indiana University in 1988, continuing the FARG research there.
The book was written during a sabbatical year at the Istituto per la Ricerca Scientifica e Tecnologica in Trento, Italy.
Publication
Upon publication, Jon Udell, a BYTE senior technical |
https://en.wikipedia.org/wiki/Leon%20Ehrenpreis | Eliezer 'Leon' Ehrenpreis (May 22, 1930 – August 16, 2010, Brooklyn) was a mathematician at Temple University who proved the Malgrange–Ehrenpreis theorem, the fundamental theorem about differential operators with constant coefficients. He previously held tenured positions at Yeshiva University and at the Courant Institute at New York University.
Early life and education
Leon was born in New York City to a family of Jewish immigrants from Eastern Europe. He graduated from Stuyvesant High School and studied Mathematics as an undergraduate at City College of New York. Afterward, he enrolled as a doctoral student at Columbia University where he studied under mathematician Claude Chevalley, obtaining his PhD in 1953 at the age of 23. His doctoral thesis was entitled "Theory of Distributions in Locally Compact Spaces".
Religion
Ehrenpreis was also a Rabbi, having received his ordination from the renowned Rabbi Moshe Feinstein. He was the author of a work on the Chumash and other religious topics, currently in manuscript.
Miscellaneous
Ehrenpreis ran the New York City Marathon every year from its inception until 2007.
Publications
See also
Ehrenpreis's fundamental principle
Ehrenpreis conjecture
References
"One thing you can count on is this math prof on the run", Temple Times, November 7, 2002 Volume 33 Number 10 (retrieved August 17, 2010)
External links
2010 deaths
1930 births
20th-century American mathematicians
21st-century American mathematicians
Jewish scientists
T |
https://en.wikipedia.org/wiki/Oscillator%20strength | In spectroscopy, oscillator strength is a dimensionless quantity that expresses the probability of absorption or emission of electromagnetic radiation in transitions between energy levels of an atom or molecule. For example, if an emissive state has a small oscillator strength, nonradiative decay will outpace radiative decay. Conversely, "bright" transitions will have large oscillator strengths. The oscillator strength can be thought of as the ratio between the quantum mechanical transition rate and the classical absorption/emission rate of a single electron oscillator with the same frequency as the transition.
Theory
An atom or a molecule can absorb light and undergo a transition from
one quantum state to another.
The oscillator strength of a transition from a lower state
to an upper state may be defined by
where is the mass of an electron and is
the reduced Planck constant. The quantum states 1,2, are assumed to have several
degenerate sub-states, which are labeled by . "Degenerate" means
that they all have the same energy .
The operator is the sum of the x-coordinates
of all electrons in the system, etc.:
The oscillator strength is the same for each sub-state .
The definition can be recast by inserting the Rydberg energy and Bohr radius
In case the matrix elements of are the same, we can get rid of the sum and of the 1/3 factor
Thomas–Reiche–Kuhn sum rule
To make equations of the previous section applicable to the states belonging to the continuum spe |
https://en.wikipedia.org/wiki/Lymphotoxin%20alpha | Lymphotoxin-alpha (LT-α) formerly known as tumor necrosis factor-beta (TNF-β) is a protein that in humans is encoded by the LTA gene. Belonging to the hematopoietic cell line, LT-α exhibits anti-proliferative activity and causes the cellular destruction of tumor cell lines. As a cytotoxic protein, LT-α performs a variety of important roles in immune regulation depending on the form that it is secreted as. Unlike other members of the TNF superfamily, LT-α is only found as a soluble homotrimer, when found at the cell surface it is found only as a heterotrimer with LTβ.
LT-α has a significant impact on the maintenance of the immune system including the development of secondary lymphoid organs. Absence of LT-α leads to the disruption of gastrointestinal development, prevents Peyer's patch development, and results in a disorganized spleen.
As a signaling molecule, LT-α is involved in the regulation of cell survival, proliferation, differentiation, and apoptosis. LT-α plays an important role in innate immune regulation and its presence has been shown to prevent tumor growth and destroy cancerous cell lines. In contrast, unregulated expression of LT-α can result in a constantly active signaling pathway, thus leading to uncontrolled cellular growth and creation of tumors. Hence depending on the context, LT-α may function to prevent growth of cancer cells or facilitate the development of tumors. Furthermore, LT-α effects depend on the type of organ it acts upon, type of cancer cel |
https://en.wikipedia.org/wiki/MCL1 | Induced myeloid leukemia cell differentiation protein Mcl-1 is a protein that in humans is encoded by the MCL1 gene.
Function
The protein encoded by this gene belongs to the Bcl-2 family. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified. The longer gene product (isoform 1) enhances cell survival by inhibiting apoptosis while the alternatively spliced shorter gene product (isoform 2) promotes apoptosis and is death-inducing. The protein MCL1 has a very short biological half-life of only 20–30 minutes.
The loss of MCL1 has a more dramatic impact than the loss of any other anti-apoptotic member of the Bcl-2 family. Loss of the Mcl-1 gene results in embryo death when the embryo is only around 3.5 days old, before it has even implanted. Conditional deletion of Mcl-1 depletes a wide variety of cells, including hematopoietic stem cells, B cell–committed progenitors, T cell–committed progenitors, antibody-secreting plasma cells, cardiac muscle cells, and neurons. Deletion of Mcl-1 in hepatocytes causes apoptosis and aberrant polyploidization but improves liver regeneration after surgery. MCL1 works synergistically with p53 in protecting liver from injury, fibrosis and cancer.
MCL1 also has a role in the cell's energy production, working in the intermitochondrial space.
Clinical significance
Omacetaxine mepesuccinate (a drug approved for the treatment for chronic myelogenous leukemia) and Seliciclib (which is u |
https://en.wikipedia.org/wiki/Psychological%20level | In finance, psychological level, is a price level in technical analysis that significantly affects the price of an underlying security, commodity or a derivative. Typically, the number is something that is "easy to remember," such as a rounded-off number. When a specific security, commodity, or derivative reaches such a price, financial market participants (traders, market makers, brokers, investors, etc.) tend to act on their positions (buy, sell or hold).
Examples
Dow Jones Industrial Average Index - $14,000.00 - the all-time high psychological thousandth level as of 11/9/2007. Also known as "Dow 14,000"
Crude Oil (light, sweet) - $100.00/barrel
References
As used by finance analysts and business reporters:
https://web.archive.org/web/20110606031923/http://www.thestreet.com/_yahoopi/markets/marketfeatures/10260856.html?cm_ven=QUIGO&cm_cat=FREE&cm_ite=NA
https://web.archive.org/web/20071114063411/http://www.tradingmarkets.com/.site/eminis/commentary/guestcommentary/-71686.cfm
http://www.dailyfx.com/story/dailyfx_reports/daily_technicals/Euro_and_Aussie_Topping__1193913286650.html
http://mobile.bloomberg.com/news/2011-12-09/euro-may-test-2001-low-versus-yen-ichimoku-suggests-technical-analysis
http://mobile.bloomberg.com/news/2011-06-30/colombia-peso-volatility-falls-as-traders-bet-on-central-bank-intervention
https://www.cnbc.com/id/45720928/Markets_May_Play_Jilted_Lover_in_Euro_Zone_Drama
http://money.cnn.com/2011/02/01/markets/markets_newyork/index.htm
External link |
https://en.wikipedia.org/wiki/Herpes%20simplex%20virus%20protein%20vmw65 | Vmw65, also known as VP16 or α-TIF (Trans Inducing Factor) is a trans-acting protein that forms a complex with the host transcription factors Oct-1 and HCF to induce immediate early gene transcription in the herpes simplex viruses.
VP16 is a strong transactivator and is often used in Y2H systems as the activation domain of the system.
References
Simplexviruses
Viral nonstructural proteins |
https://en.wikipedia.org/wiki/XRCC3 | DNA repair protein XRCC3 is a protein that in humans is encoded by the XRCC3 gene.
Function
This gene encodes a member of the RecA/Rad51-related protein family that participates in homologous recombination to maintain chromosome stability and repair DNA damage. This gene functionally complements Chinese hamster irs1SF, a repair-deficient mutant that exhibits hypersensitivity to a number of different DNA-damaging agents and is chromosomally unstable. A rare microsatellite polymorphism in this gene is associated with cancer in patients of varying radiosensitivity.
The XRCC3 protein is one of five paralogs of RAD51, including RAD51B (RAD51L1), RAD51C (RAD51L2), RAD51D (RAD51L3), XRCC2 and XRCC3. They each share about 25% amino acid sequence identity with RAD51 and each other.
The RAD51 paralogs are all required for efficient DNA double-strand break repair by homologous recombination and depletion of any paralog results in significant decreases in homologous recombination frequency.
Two paralogs form a complex designated CX3 (RAD51C-XRCC3). Four paralogs form a second complex designated BCDX2 (RAD51B-RAD51C-RAD51D-XRCC2). These two complexes act at two different stages of homologous recombinational DNA repair.
The CX3 complex acts downstream of RAD51, after its recruitment to damage sites. The CX3 complex associates with Holliday junction resolvase activity, probably in a role of stabilizing gene conversion tracts.
The BCDX2 complex is responsible for RAD51 recruitmen |
https://en.wikipedia.org/wiki/Interleukin%201%20receptor%2C%20type%20II | Interleukin 1 receptor, type II (IL-1R2) also known as CD121b (Cluster of Differentiation 121b) is an interleukin receptor. IL1R2 also denotes its human gene.
Function
The protein encoded by this gene is a decoy receptor for certain cytokines that belongs to the interleukin-1 receptor family. This protein binds interleukin-1α (IL1A), interleukin-1β (IL1B), and interleukin 1 receptor antagonist (IL1Ra), preventing them from binding to their regular receptors and thereby inhibiting the transduction of their signaling. IL-1R2 protein also interacts non-productively with the second component of the signaling IL-1 receptor, namely IL-1RAcP, and a complex of the IL-1R2 and IL-1RAcP extracellular domains with interleukin-1 beta has been solved by X-ray crystallography. Interleukin 4 (IL4) is reported to antagonize the activity of interleukin 1 by inducing the expression and release of this cytokine. This gene and three other genes form a cytokine receptor gene cluster on chromosome 2q12. Two alternatively spliced transcript variants encoding the same protein have been reported.
See also
Cluster of differentiation
Interleukin 1 receptor, type I
References
Further reading
External links
Immunoglobulin superfamily cytokine receptors
Clusters of differentiation |
https://en.wikipedia.org/wiki/HIST1H3B | Histone H3.1 is a protein that in humans is encoded by the H3C2 gene.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6p22-p21.3.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Methyl-CpG-binding%20domain%20protein%202 | Methyl-CpG-binding domain protein 2 is a protein that in humans is encoded by the MBD2 gene.
Function
DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG-binding domain (MBD). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MECP2, MBD1, and MBD2 can also repress transcription from methylated gene promoters. The protein encoded by these genes may function as a mediator of the biological consequences of the methylation signal. It is also reported that MBD2 and MBD3 recruit the NuRD complex to regions of DNA depending on their selective binding of methylated CpG sites. Therefore, MBD2/NuRD and MBD3/NuRD define two distinct protein complexes with different biochemical and functional properties.
Interactions
Methyl-CpG-binding domain protein 2 has been shown to interact with:
GATAD2B,
HDAC1,
Histone deacetylase 2,
MBD3
MIZF, and
SIN3A.
References
Further reading
Human proteins |
https://en.wikipedia.org/wiki/MTA1 | Metastasis-associated protein MTA1 is a protein that in humans is encoded by the MTA1 gene. MTA1 is the founding member of the MTA family of genes. MTA1 is primarily localized in the nucleus but also found to be distributed in the extra-nuclear compartments. MTA1 is a component of several chromatin remodeling complexes including the nucleosome remodeling and deacetylation complex (NuRD). MTA1 regulates gene expression by functioning as a coregulator to integrate DNA-interacting factors to gene activity. MTA1 participates in physiological functions in the normal and cancer cells. MTA1 is one of the most upregulated proteins in human cancer and associates with cancer progression, aggressive phenotypes, and poor prognosis of cancer patients.
Discovery
MTA1 was first cloned by Toh, Pencil and Nicholson in 1994 as a differentially expressed gene in a highly metastatic rat breast cancer cell line. The role in MTA1 in chromatin remodeling was deduced due to the presence of MTA1 polypeptides in the NuRD complex. The first direct target of the MTA1-NuRD complex was ERα. MTA2 was initially recognized as MTA1-like 1 gene, named as MTA1-L1, as a randomly selected clone from a large-scale sequencing effort of human cDNAs by Takashi Tokino's laboratory. MTA2's suspected role in chromatin remodeling was inferred from the prevalence of MTA2 polypeptides with the NuRD complex in a proteomic study(Zhang et al., 1999, Kumar and Wang, 2016).
Gene and spliced variants
The MTA1 is 715/703 |
https://en.wikipedia.org/wiki/CD163 | CD163 (Cluster of Differentiation 163) is a protein that in humans is encoded by the CD163 gene. CD163 is the high affinity scavenger receptor for the hemoglobin-haptoglobin complex and in the absence of haptoglobin - with lower affinity - for hemoglobin alone. It also is a marker of cells from the monocyte/macrophage lineage. CD163 functions as innate immune sensor for gram-positive and gram-negative bacteria. The receptor was discovered in 1987.
Structure
The molecular size is 130 kDa. The receptor belongs to the scavenger receptor cysteine rich family type B and consists of a 1048 amino acid residues extracellular domain, a single transmembrane segment and a cytoplasmic tail with several splice variants.
Clinical significance
A soluble form of the receptor exists in plasma, and cerebrospinal fluid., commonly denoted sCD163. It is generated by ectodomain shedding of the membrane bound receptor, which may represent a form of modulation of CD163 function. sCD163 shedding occurs as a result of enzymatic cleavage by ADAM17. sCD163 is upregulated in a large range of inflammatory diseases including liver cirrhosis, type 2 diabetes, macrophage activation syndrome, Gaucher's disease, sepsis, HIV infection, rheumatoid arthritis and Hodgkin Lymphoma. sCD163 is also upregulated in cerebrospinal fluid after subarachnoid haemorrhage. CD163 has recently been identified as expressed on neurons in the CNS following hemorrhage, although the significance of this is unclear. The excreti |
https://en.wikipedia.org/wiki/RBX1 | RING-box protein 1 is a protein that in humans is encoded by the RBX1 gene.
Function
This gene encodes an evolutionarily conserved protein that interacts with cullins. The protein plays a unique role in the ubiquitination reaction by heterodimerizing with cullin-1 to catalyze ubiquitin polymerization. It also may be involved in the regulation of protein turn-over.
Interactions
RBX1 has been shown to interact with:
CAND1,
CUL1,
CUL2,
CUL4A,
CUL5
CUL7,
DCUN1D1, and
P70-S6 Kinase 1.
References
Further reading |
https://en.wikipedia.org/wiki/ATF4 | Activating transcription factor 4 (tax-responsive enhancer element B67), also known as ATF4, is a protein that in humans is encoded by the ATF4 gene.
Function
This gene encodes a transcription factor that was originally identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV-1. The encoded protein was also isolated and characterized as the cAMP-response element binding protein 2 (CREB-2). ATF4 is not a functional transcription factor by itself but one-half of many possible heterodimeric transcription factors. Because ATF4 can simultaneously participate in multiple distinct heterodimers, the overall set of genes that require ATF4 for maximal expression in a specific context (ATF4-dependent genes) can be a mixture of genes that are regulated by different ATF4 heterodimers, with some ATF4-dependent genes activated by one ATF4 heterodimer and other ATF4-dependent genes activated by other ATF4 heterodimers.
The protein encoded by this gene belongs to a family of DNA-binding proteins that includes the AP-1 family of transcription factors, cAMP-response element binding proteins (CREBs) and CREB-like proteins. These transcription factors share a leucine zipper region that is involved in protein–protein interactions, located C-terminal to a stretch of basic amino acids that functions as a DNA-binding domain. Two alternative transcripts encoding the same protein have been described. Two pseudogenes are loc |
https://en.wikipedia.org/wiki/BCL3 | B-cell lymphoma 3-encoded protein is a protein that in humans is encoded by the BCL3 gene.
This gene is a proto-oncogene candidate. It is identified by its translocation into the immunoglobulin alpha-locus in some cases of B-cell leukemia. The protein encoded by this gene contains seven ankyrin repeats, which are most closely related to those found in I kappa B proteins. This protein functions as a transcriptional coactivator that activates through its association with NF-kappa B homodimers. The expression of this gene can be induced by NF-kappa B, which forms a part of the autoregulatory loop that controls the nuclear residence of p50 NF-kappa B.
Like BCL2, BCL5, BCL6, BCL7A, BCL9, and BCL10, it has clinical significance in lymphoma.
Interactions
BCL3 has been shown to interact with:
BARD1,
C-Fos,
C-jun,
C22orf25,
COPS5,
EP300,
HTATIP,
NFKB1,
NFKB2,
PIR, and
NR2B1.
Clinical significance
Genetic variations in BCL3 gene have been associated with late-onset Alzheimer's disease (LOAD) and chronic lymphocytic leukemia. β-amyloid accumulation in neurons of Alzheimer's patients results in activation of NF-κB, which induces BCL3 expression. Increased expression of BCL3 has been observed in the brains of patients with LOAD.
The role of Bcl3 in solid tumors was established through the ability of Bcl3 to promote metastasis without affecting primary tumor growth or normal mammary function, within models of ErbB2-positive breast cancer. Further research has uncovere |
https://en.wikipedia.org/wiki/HSD17B1 | 17β-Hydroxysteroid dehydrogenase 1 (17β-HSD1) is an enzyme that in humans is encoded by the HSD17B1 gene. This enzyme oxidizes or reduces the C17 hydroxy/keto group of androgens and estrogens and hence is able to regulate the potency of these sex steroids
Function
This enzyme is responsible for the interconversion of estrone (E1) and estradiol (E2) and for the interconversion of androstenedione and testosterone:
17β-estradiol + NADP+ + estrone + NADPH + H+
testosterone + NADP+ + androstenedione + NADPH + H+
The human 17β-HSD1 isozyme is highly specific for estrogens over androgens whereas the rodent isozyme is less specific.
Discovery
Human 17β-HSD1 was the first enzyme of the 17β-HSD family to be cloned and to have its sequence identified. Its three-dimensional structure is also the first example of any human steroid-converting enzyme.
Structure
This enzyme contains a short-chain dehydrogenase domain that contains a characteristic 3-layer (αβα) sandwich known as a Rossmann fold. The human enzyme contains 327 amino acids and exists as a homodimer with two identical subunits of 34.5 kDa The N-terminal short-chain dehydrogenase domain contains binding site for the NADP+/NADPH cofactor. A narrow, hydrophobic C-terminal domain contains a binding pocket for the steroid substrate.
Clinical significance
Estradiol stimulates while dihydrotestosterone (DHT) inhibits breast cancer growth. Furthermore 17β-HSD1 levels positively correlate with estradiol and negatively correlat |
https://en.wikipedia.org/wiki/HTR3A | 5-hydroxytryptamine receptor 3A is a protein that in humans is encoded by the HTR3A gene.
The product of this gene belongs to the ligand-gated ion channel receptor superfamily. This gene encodes subunit A of the type 3 receptor for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor causes fast, depolarizing responses in neurons after activation. The A subunit is the only one that can be expressed alone and forms homomers with a very low single channel conductance of 0.6pS. When combined with the B subunit and expressed as a heteromer, the single channel conductance increases immensely. Alternatively spliced transcript variants encoding different isoforms have been identified.
See also
5-HT3 receptor
References
Further reading
External links
Ion channels
Serotonin receptors |
https://en.wikipedia.org/wiki/IFNAR2 | Interferon-alpha/beta receptor beta chain is a protein that in humans is encoded by the IFNAR2 gene.
Function
The protein encoded by this gene is a type I membrane protein that forms one of the two chains of a receptor for interferons alpha and beta. Binding and activation of the receptor stimulates Janus protein kinases, which in turn phosphorylate several proteins, including STAT1 and STAT2. Multiple transcript variants encoding at least two different isoforms have been found for this gene.
Interactions
IFNAR2 has been shown to interact with:
GNB2L1,
IFNA2,
STAT1, and
STAT2.
References
Further reading |
https://en.wikipedia.org/wiki/LAMP2 | Lysosome-associated membrane protein 2 (LAMP2), also known as CD107b (Cluster of Differentiation 107b) and Mac-3, is a human gene. Its protein, LAMP2, is one of the lysosome-associated membrane glycoproteins.
The protein encoded by this gene is a member of a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands. It may play a role in tumor cell metastasis. It may also function in the protection, maintenance, and adhesion of the lysosome. Alternative splicing of the gene produces three variants - LAMP-2A, LAMP-2B and LAMP-2C. LAMP-2A is the receptor for chaperone-mediated autophagy. Recently it has been determined that antibodies against LAMP-2 account for a fraction of patients who get a serious kidney disease termed focal necrotizing glomerulonephritis.
LAMP-2B is associated with Danon disease.
Structure and tissue distribution
The gene for LAMP2 has 9 coding exons and 2 alternate last exons, 9a and 9b. When the last exon is spliced with the alternative exon, it is a variant called LAMP2b, which varies in the last 11 amino acids of its C-terminal sequence: in the luminal domain, the transmembrane domain, and the cytoplasmic tail. The original (LAMP2a) is highly expressed in the placenta, lung, and liver, while LAMP2b is highly expressed in skeletal muscle.
Function
Lysosomes are cell organelles found in most animal cells. Their main functions center around breaking down materials and debris in the cell. Some of this is d |
https://en.wikipedia.org/wiki/NFYA | Nuclear transcription factor Y subunit alpha is a protein that in humans is encoded by the NFYA gene.
Function
The protein encoded by this gene is one subunit of a trimeric complex NF-Y, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit NFYA associates with a tight dimer composed of the NFYB and NFYC subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the NFYA subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.
NF-Y complex serves as a pioneer factor by promoting chromatin accessibility to facilitate other co-localizing cell type-specific transcription factors.
NF-Y has also been implicated as a central player in transcription start site (TSS) selection in animals. It safeguards the integrity of the nucleosome-depleted region and PIC localization at protein-coding gene promoters.
Interactions
NFYA has been shown to interact with Serum response factor and ZHX1. NFYA, NFYB and NFYC form the NFY complex and it has been shown that the NFY complex serves as a pioneer factor by promoting chromatin ac |
https://en.wikipedia.org/wiki/P2RY1 | P2Y purinoceptor 1 is a protein that in humans is encoded by the P2RY1 gene.
Function
The product of this gene, P2Y1 belongs to the family of G-protein coupled receptors. This family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. This receptor functions as a receptor for extracellular ATP and ADP. In platelets binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and probably to platelet aggregation.
See also
P2Y receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/PEX5 | Peroxisomal targeting signal 1 receptor (PTS1R) is a protein that in humans is encoded by the PEX5 gene.
PTS1R is a peroxisomal targeting sequence involved in the specific transport of molecules for oxidation inside the peroxisome. SKL binds to PTS1R in the cytosol followed by binding to the Pex14p receptor allowing importation of the peroxisomal protein through the pexsubunit transporter.
Diseases associated with dysfunctional PTS1R receptors include X-linked adrenoleukodystrophy and Zellweger syndrome.
Interactions
PEX5 has been shown to interact with PEX12, PEX13 and PEX14.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Peroxisome Biogenesis Disorders, Zellweger Syndrome Spectrum
OMIM entries on Peroxisome Biogenesis Disorders, Zellweger Syndrome Spectrum |
https://en.wikipedia.org/wiki/SUPT5H | Transcription elongation factor SPT5 is a protein that in humans is encoded by the SUPT5H gene.
Interactions
SUPT5H has been shown to interact with:
CDK9,
Cyclin-dependent kinase 7,
HTATSF1,
PIN1,
POLR2A,
PRMT1 and
Protein arginine methyltransferase 5.
Model organisms
Model organisms have been used in the study of SUPT5H function. A conditional knockout mouse line called Supt5tm2a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed: - In-depth immunological phenotyping
References
Further reading |
https://en.wikipedia.org/wiki/ELOC | Elongin C is a protein that in humans is encoded by the ELOC gene.
Function
Elongin C is a subunit of the transcription factor B (SIII) complex. The SIII complex is composed of elongins A/A2, B and C. It activates elongation by RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin A functions as the transcriptionally active component of the SIII complex, whereas elongins B and C are regulatory subunits. Elongin A2 is specifically expressed in the testis, and capable of forming a stable complex with elongins B and C. The von Hippel-Lindau tumor suppressor protein binds to elongins B and C, and thereby inhibits transcription elongation.
Interactions
TCEB1 has been shown to interact with:
TCEB2 and
Von Hippel-Lindau tumor suppressor.
References
Further reading |
https://en.wikipedia.org/wiki/XTAR | XTAR, LLC is a commercial satellite operator exclusively providing services in the X band frequency range, which is the communications cornerstone of today's military, diplomatic, humanitarian and emergency disaster response operations. A privately owned and operated company, XTAR supports the critical satellite communications needs of governments around the world through its two X-band payloads. The XTAR satellites were designed and built by private financing. Loral Space & Communications, Inc. owns the majority share. XTAR is headquartered in Ashburn, VA.
With its high-powered 72 MHz transponders and global, fixed and steerable beams, XTAR provides over 4 GB of secure X-band capacity with coverage from Denver east to Singapore. The system can accommodate massive wideband data requirements and provides overlapping coverage with regional redundancy for increased service and reliability.
XTAR bandwidth is not application-specific; it can support and transmit to any one of the primary architectures used by government agencies today, including fixed-to-fixed, tactical-to-tactical, reach-back, broadcast and airborne platforms.
In 2019, XTAR and Spanish governmental satellite operator Hisdesat announced plans to construct two new military communications satellites. The new 'Next Generation' satellites will include X-band and military Ka-band capacity.
Satellite Fleet
The XTAR fleet uses the hosted payload model, an application that is becoming increasingly used by U.S. and o |
https://en.wikipedia.org/wiki/Adaptor-related%20protein%20complex%202%2C%20alpha%201 | AP-2 complex subunit alpha-1 is a protein that in humans is encoded by the AP2A1 gene.
This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP2 adaptors) complex found in clathrin coated vesicles. The AP-2 complex is a heterotetramer consisting of two large adaptins (alpha or beta), a medium adaptin (mu), and a small adaptin (sigma). The complex is part of the protein coat on the cytoplasmic face of coated vesicles which links clathrin to receptors in vesicles. Alternative splicing of this gene results in two transcript variants encoding two different isoforms. A third transcript variant has been described, but its full length nature has not been determined.
Interactions
Adaptor-related protein complex 2, alpha 1 has been shown to interact with DPYSL2 and NUMB.
References
Further reading
External links |
https://en.wikipedia.org/wiki/DAZL | Deleted in azoospermia-like is a protein that in humans is encoded by the DAZL gene.
Function
The DAZ (Deleted in AZoospermia) gene family encodes potential RNA binding proteins that are expressed in prenatal and postnatal germ cells of males and females. The protein encoded by this gene is localized to the nucleus and cytoplasm of fetal germ cells and to the cytoplasm of developing oocytes. In the testis, this protein is localized to the nucleus of spermatogonia but relocates to the cytoplasm during meiosis where it persists in spermatids and spermatozoa. Transposition and amplification of this autosomal gene during primate evolution gave rise to the DAZ gene cluster on the Y chromosome. Mutations in this gene have been linked to severe spermatogenic failure and infertility in males.
In mice and pigs deficient in DAZL, PGCs migrate to the gonad but do not undertake germ cell determination, and may instead produce germ cell tumors.
Interactions
DAZL has been shown to interact with DAZ1.
References
Further reading |
https://en.wikipedia.org/wiki/Transferrin%20receptor%202 | Transferrin receptor 2 (TfR2) is a protein that in humans is encoded by the TFR2 gene. This protein is involved in the uptake of transferrin-bound iron into cells by endocytosis, although its role is minor compared to transferrin receptor 1.
Function
This gene is a member of the transferrin receptor-like family and encodes a single-pass type II membrane protein with a protease associated (PA) domain, an M28 peptidase domain and a transferrin receptor-like dimerization domain. This protein mediates cellular uptake of transferrin-bound iron and mutations in this gene have been associated with hereditary hemochromatosis type III. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.
See also
Transferrin receptor 1
Transferrin
References
Further reading
External links
GeneReviews/NIH/NCBI/UW entry on TFR2-Related or Type 3 Hereditary Hemochromatosis
Iron metabolism
Transferrins |
https://en.wikipedia.org/wiki/RAB11A | Ras-related protein Rab-11A is a protein that in humans is encoded by the RAB11A gene.
Function
The protein encoded by this gene belongs to the small GTPase superfamily, Rab family. It is associated with both constitutive and regulated secretory pathways, and may be involved in protein transport.
Rab-11a controls intracellular trafficking of the innate immune receptor TLR4, and thereby also receptor signaling
Interactions
RAB11A has been shown to interact with:
RAB11FIP1,
RAB11FIP2,
RAB11FIP3,
RAB11FIP4, and
RAB11FIP5
Moesin
References
Further reading |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.