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https://en.wikipedia.org/wiki/Isoorientin%203%27-O-methyltransferase | In enzymology, an isoorientin 3'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + isoorientin S-adenosyl-L-homocysteine + isoscoparin
Thus, the two substrates of this enzyme are S-adenosyl methionine and isoorientin, whereas its two products are S-adenosylhomocysteine and isoscoparin.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:isoorientin 3'-O-methyltransferase. This enzyme is also called isoorientin 3'-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure
O-methylated flavones metabolism |
https://en.wikipedia.org/wiki/Jasmonate%20O-methyltransferase | In enzymology, a jasmonate O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + jasmonate S-adenosyl-L-homocysteine + methyl jasmonate
Thus, the two substrates of this enzyme are S-adenosyl methionine and jasmonate, whereas its two products are S-adenosylhomocysteine and methyl jasmonate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:jasmonate O-methyltransferase. This enzyme is also called jasmonic acid carboxyl methyltransferase.
References
Further reading
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Kaempferol%204%27-O-methyltransferase | In enzymology, a kaempferol 4'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + kaempferol S-adenosyl-L-homocysteine + kaempferide
Thus, the two substrates of this enzyme are S-adenosyl methionine and kaempferol, whereas its two products are S-adenosylhomocysteine and kaempferide.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:kaempferol 4'-O-methyltransferase. Other names in common use include S-adenosyl-L-methionine:flavonoid 4'-O-methyltransferase, and F 4'-OMT.
References
EC 2.1.1
Enzymes of unknown structure
Kaempferol
Flavonols metabolism
O-methylated flavonoids metabolism |
https://en.wikipedia.org/wiki/Licodione%202%27-O-methyltransferase | In enzymology, a licodione 2'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + licodione S-adenosyl-L-homocysteine + 2'-O-methyllicodione
Thus, the two substrates of this enzyme are S-adenosyl methionine and licodione, whereas its two products are S-adenosylhomocysteine and 2'-O-methyllicodione.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:licodione 2'-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Loganate%20O-methyltransferase | In enzymology, a loganate O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + loganic acid S-adenosyl-L-homocysteine + loganin
Thus, the two substrates of this enzyme are S-adenosyl methionine and loganic acid (also called loganate), whereas its two products are S-adenosylhomocysteine and loganin.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:loganate 11-O-methyltransferase. Other names in common use include loganate methyltransferase, and S-adenosyl-L-methionine:loganic acid methyltransferase. This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Luteolin%20O-methyltransferase | In enzymology, a luteolin O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5,7,3',4'-tetrahydroxyflavone (luteolin), whereas its two products are S-adenosylhomocysteine and 5,7,4'-trihydroxy-3'-methoxyflavone.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:5,7,3',4'-tetrahydroxyflavone 3'-O-methyltransferase. Other names in common use include o-dihydric phenol methyltransferase, luteolin methyltransferase, luteolin 3'-O-methyltransferase, o-diphenol m-O-methyltransferase, o-dihydric phenol meta-O-methyltransferase, and S-adenosylmethionine:flavone/flavonol 3'-O-methyltransferase. This enzyme participates in flavonoid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure
O-methylated flavones metabolism |
https://en.wikipedia.org/wiki/Macrocin%20O-methyltransferase | In enzymology, a macrocin O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + macrocin S-adenosyl-L-homocysteine + tylosin
Thus, the two substrates of this enzyme are S-adenosyl methionine and macrocin, whereas its two products are S-adenosylhomocysteine and tylosin.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:macrocin 3"'-O-methyltransferase. Other names in common use include macrocin methyltransferase, and S-adenosyl-L-methionine-macrocin O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Magnesium%20protoporphyrin%20IX%20methyltransferase | In enzymology, a magnesium protoporphyrin IX methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + magnesium protoporphyrin IX S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
The two substrates of this enzyme are S-adenosyl methionine and magnesium protoporphyrin IX; its two products are S-adenosylhomocysteine and magnesium protoporphyrin IX 13-methyl ester.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:magnesium-protoporphyrin-IX O-methyltransferase. This enzyme is part of the biosynthetic pathway to chlorophylls.
See also
Biosynthesis of chlorophylls
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methanol%E2%80%945-hydroxybenzimidazolylcobamide%20Co-methyltransferase | In enzymology, a methanol-5-hydroxybenzimidazolylcobamide Co-methyltransferase () is an enzyme that catalyzes the chemical reaction
methanol + 5-hydroxybenzimidazolylcobamide Co-methyl-Co-5-hydroxybenzimidazolylcob(I)amide + H2O
Thus, the two substrates of this enzyme are methanol and 5-hydroxybenzimidazolylcobamide, whereas its two products are Co-methyl-Co-5-hydroxybenzimidazolylcob(I)amide and H2O.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is methanol:5-hydroxybenzimidazolylcobamide Co-methyltransferase. Other names in common use include methanol cobalamin methyltransferase, methanol:5-hydroxybenzimidazolylcobamide methyltransferase, and MT 1.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
Further reading
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methionine%20S-methyltransferase | In enzymology, a methionine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + L-methionine S-adenosyl-L-homocysteine + S-methyl-L-methionine
Thus, the two substrates of this enzyme are S-adenosyl methionine and L-methionine, whereas its two products are S-adenosylhomocysteine and S-methyl-L-methionine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:L-methionine S-methyltransferase. Other names in common use include S-adenosyl methionine:methionine methyl transferase, methionine methyltransferase, S-adenosylmethionine transmethylase, and S-adenosylmethionine-methionine methyltransferase. This enzyme participates in selenoamino acid metabolism. It has 2 cofactors: manganese, and zinc.
References
EC 2.1.1
Manganese enzymes
Zinc enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylamine%E2%80%94glutamate%20N-methyltransferase | In enzymology, a methylamine-glutamate N-methyltransferase () is an enzyme that catalyzes the chemical reaction
methylamine + -glutamate NH3 + N-methyl--glutamate
Thus, the two substrates of this enzyme are methylamine and -glutamate, whereas its two products are NH3 and N-methyl--glutamate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is methylamine:-glutamate N-methyltransferase. Other names in common use include N-methylglutamate synthase, and methylamine-glutamate methyltransferase. This enzyme participates in methane metabolism.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylated-DNA%E2%80%94%28protein%29-cysteine%20S-methyltransferase | In enzymology, a methylated-DNA-[protein]-cysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
DNA (containing 6-O-methylguanine) + protein L-cysteine DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine
Thus, the two substrates of this enzyme are DNA containing 6-O-methylguanine and protein L-cysteine, whereas its two products are DNA and protein S-methyl-L-cysteine. The S-methyl-L-cysteine residue irreversibly inactivates the protein, allowing only one transfer for each protein.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is DNA-6-O-methylguanine:[protein]-L-cysteine S-methyltransferase.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methylene-fatty-acyl-phospholipid%20synthase | In enzymology, a methylene-fatty-acyl-phospholipid synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + phospholipid olefinic fatty acid S-adenosyl-L-homocysteine + phospholipid methylene fatty acid
Thus, the two substrates of this enzyme are S-adenosyl methionine and phospholipid olefinic fatty acid, whereas its two products are S-adenosylhomocysteine and phospholipid methylene fatty acid.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:unsaturated-phospholipid methyltransferase (methenylating). This enzyme is also called unsaturated-phospholipid methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylenetetrahydrofolate%E2%80%94tRNA-%28uracil-5-%29-methyltransferase | In enzymology, a methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2 tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, tRNA containing uridine at position 54, and FADH2, whereas its 3 products are tetrahydrofolate, tRNA containing ribothymidine at position 54, and FAD.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:tRNA (uracil-5-)-methyl-transferase. Other names in common use include (FADH2-oxidizing), folate-dependent ribothymidyl synthase, methylenetetrahydrofolate-transfer ribonucleate uracil, 5-methyltransferase, 5,10-methylenetetrahydrofolate:tRNA-UPsiC, and (uracil-5-)-methyl-transferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylquercetagetin%206-O-methyltransferase | In enzymology, a methylquercetagetin 6-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 5,6,3',4'-tetrahydroxy-3,7-dimethoxyflavone S-adenosyl-L-homocysteine + 5,3',4'-trihydroxy-3,6,7-trimethoxyflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5,6,3',4'-tetrahydroxy-3,7-dimethoxyflavone, whereas its two products are S-adenosylhomocysteine and 5,3',4'-trihydroxy-3,6,7-trimethoxyflavone.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone 6-O-methyltransferase. Other names in common use include flavonol 6-O-methyltransferase, flavonol 6-methyltransferase, 6-OMT, S-adenosyl-L-methionine:3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone, and 6-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/MRNA%20%282%27-O-methyladenosine-N6-%29-methyltransferase | In enzymology, a mRNA (2'-O-methyladenosine-N6-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + m7G(5')pppAm S-adenosyl-L-homocysteine + m7G(5')pppm6Am (mRNA containing an N6,2'-O-dimethyladenosine cap)
Thus, the two substrates of this enzyme are S-adenosyl methionine and m7G(5')pppAm, whereas its two products are S-adenosylhomocysteine and m7G(5')pppm6Am (mRNA containing an N6,2'-O-dimethyladenosine cap).
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:mRNA (2'-O-methyladenosine-N6-)-methyltransferase. Other names in common use include messenger ribonucleate 2'-O-methyladenosine NG-methyltransferase, S-adenosyl-L-methionine:mRNA, and (2'-O-methyladenosine-6-N-)-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/MRNA%20%28guanine-N7-%29-methyltransferase | In enzymology, a mRNA (guanine-N7-)-methyltransferase also known as mRNA cap guanine-N7 methyltransferase is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + G(5')pppR-RNA S-adenosyl-L-homocysteine + m7G(5')pppR-RNA (mRNA containing an N7-methylguanine cap)
Thus, the two substrates of this enzyme are S-adenosyl methionine and G(5')pppR-RNA, whereas its two products are S-adenosylhomocysteine and m7G(5')pppR-RNA. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases.
In humans, mRNA cap guanine-N7 methyltransferase is encoded by the RNMT gene.
Nomenclature
The systematic name of this enzyme class is S-adenosyl-L-methionine:mRNA (guanine-N7-)-methyltransferase. Other names in common use include:
messenger ribonucleate guanine 7-methyltransferase,
guanine-7-methyltransferase,
messenger RNA guanine 7-methyltransferase, and
S-adenosyl-L-methionine:mRNA (guanine-7-N-)-methyltransferase.
cap MTase
See also
7-Methylguanosine
References
Further reading
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/MRNA%20%28nucleoside-2%27-O-%29-methyltransferase | In enzymology, a mRNA (nucleoside-2'-O-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + m7G(5')pppR-RNA S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA (mRNA containing a 2'-O-methylpurine cap)
Thus, the two substrates of this enzyme are S-adenosyl methionine and m7G(5')pppR-RNA, whereas its two products are S-adenosylhomocysteine and m7G(5')pppRm-RNA (mRNA containing a 2'-O-methylpurine cap).
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:mRNA (nucleoside-2'-O-)-methyltransferase. Other names in common use include messenger ribonucleate nucleoside 2'-methyltransferase, and messenger RNA (nucleoside-2'-)-methyltransferase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28Myelin%20basic%20protein%29-arginine%20N-methyltransferase | In enzymology, a [myelin basic protein]-arginine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + [myelin basic protein]-arginine S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-arginine
Thus, the two substrates of this enzyme are S-adenosyl methionine and myelin basic protein-arginine, whereas its two products are S-adenosylhomocysteine and myelin basic protein-Nomega-methyl-arginine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:[myelin-basic-protein]-arginine Nomega-methyltransferase. Other names in common use include myelin basic protein methylase I, protein methylase I, S-adenosyl-L-methionine:[myelin-basic-protein]-arginine, and omega-N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Myricetin%20O-methyltransferase | In enzymology, a myricetin O-methyltransferase () is an enzyme that catalyzes the chemical reaction
2 S-adenosyl-L-methionine + myricetin 2 S-adenosyl-L-homocysteine + syringetin
Thus, the two substrates of this enzyme are S-adenosyl methionine and myricetin, whereas its two products are S-adenosylhomocysteine and syringetin.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:myricetin O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure
Flavonols metabolism
O-methylated flavonoids metabolism |
https://en.wikipedia.org/wiki/GSTT1 | Glutathione S-transferase theta-1 is an enzyme that in humans is encoded by the GSTT1 gene.
Glutathione S-transferase (GST) theta 1 (GSTT1) is a member of a superfamily of proteins that catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. Human GSTs can be divided into five main classes: alpha, mu, pi, theta, and zeta. The theta class includes GSTT1 and GSTT2. The GSTT1 and GSTT2 share 55% amino acid sequence identity and both of them were claimed to have an important role in human carcinogenesis. The GSTT1 gene is located approximately 50kb away from the GSTT2 gene. The GSTT1 and GSTT2 genes have a similar structure, being composed of five exons with identical exon/intron boundaries.
References
Enzymes
Genes |
https://en.wikipedia.org/wiki/N-benzoyl-4-hydroxyanthranilate%204-O-methyltransferase | In enzymology, a N-benzoyl-4-hydroxyanthranilate 4-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + N-benzoyl-4-hydroxyanthranilate S-adenosyl-L-homocysteine + N-benzoyl-4-methoxyanthranilate
Thus, the two substrates of this enzyme are S-adenosyl methionine and N-benzoyl-4-hydroxyanthranilate, whereas its two products are S-adenosylhomocysteine and N-benzoyl-4-methoxyanthranilate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:N-benzoyl-4-O-hydroxyanthranilate 4-O-methyltransferase. Other names in common use include N-benzoyl-4-hydroxyanthranilate 4-methyltransferase, and benzoyl-CoA:anthranilate N-benzoyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nicotinamide%20N-methyltransferase | In enzymology, a nicotinamide N-methyltransferase (NNMT) () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + nicotinamide S-adenosyl-L-homocysteine + 1-methylnicotinamide.
Thus, the two substrates of this enzyme are S-adenosyl methionine and nicotinamide, whereas its two products are S-adenosylhomocysteine and 1-methylnicotinamide.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:nicotinamide N-methyltransferase. This enzyme is also called nicotinamide methyltransferase.
Function
This enzyme participates in nicotinate and nicotinamide metabolism.
NNMT affects a biochemical mechanism known as a futile cycle, which plays a role in metabolic regulation. NNMT is found in human fat cells and the liver. NNMT processes vitamin B3 and has been linked with certain types of cancer. Silencing the gene that codes for NNMT reduces its presence and increases the presence of sugar transporter GLUT4.
Mice that produced large amounts of GLUT4 were insulin sensitive and protected against diabetes, while mice with no GLUT4 were insulin resistant and at risk. High levels of NNMT are often found in the fat cells of animals that are insulin resistant. When the researchers silenced the NNMT gene in mice on high-fat diets, the mice gained less weight than those in whom the NNMT gene was functioning normally. (The mice did not |
https://en.wikipedia.org/wiki/Nicotinate%20N-methyltransferase | In enzymology, a nicotinate N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + nicotinate S-adenosyl-L-homocysteine + N-methylnicotinate
Thus, the two substrates of this enzyme are S-adenosyl methionine and nicotinate, whereas its two products are S-adenosylhomocysteine and N-methylnicotinate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:nicotinate N-methyltransferase. Other names in common use include furanocoumarin 8-methyltransferase, and furanocoumarin 8-O-methyltransferase. This enzyme participates in nicotinate and nicotinamide 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 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Anaphylatoxin%20receptors | The anaphylatoxin receptors are a group of G-protein coupled receptors which bind anaphylatoxins. Members of this family include:
C3a receptor
C5a receptor
C5L2
References
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/HSPA1A | Heat shock 70 kDa protein 1, also termed Hsp72, is a protein that in humans is encoded by the HSPA1A gene. As a member of the heat shock protein 70 family and a chaperone protein, it facilitates the proper folding of newly translated and misfolded proteins, as well as stabilize or degrade mutant proteins. In addition, Hsp72 also facilitates DNA repair. Its functions contribute to biological processes including signal transduction, apoptosis, protein homeostasis, and cell growth and differentiation. It has been associated with an extensive number of cancers, neurodegenerative diseases, cell senescence and aging, and inflammatory diseases such as Diabetes mellitus type 2 and rheumatoid arthritis.
Structure
This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 (Hsp70) family. As a Hsp70 protein, it has a C-terminal protein substrate-binding domain and an N-terminal ATP-binding domain.
The substrate-binding domain consists of two subdomains, a two-layered β-sandwich subdomain (SBDβ) and an α-helical subdomain (SBDα), which are connected by the loop Lα,β. SBDβ contains the peptide binding pocket while SBDα serves as a lid to cover the substrate binding cleft. The ATP binding domain consists of four subdomains split into two lobes by a central ATP/ADP binding pocket. The two terminal domains are linked together by a conserved region referred to as loop LL,1, which is critical for allosteric regulation. The unstructured region at |
https://en.wikipedia.org/wiki/O-demethylpuromycin%20O-methyltransferase | In enzymology, an O-demethylpuromycin O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + O-demethylpuromycin S-adenosyl-L-homocysteine + puromycin
Thus, the two substrates of this enzyme are S-adenosyl methionine and O-demethylpuromycin, whereas its two products are S-adenosylhomocysteine and puromycin.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:O-demethylpuromycin O-methyltransferase. This enzyme is also called O-demethylpuromycin methyltransferase. This enzyme participates in puromycin biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenol%20O-methyltransferase | In enzymology, a phenol O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + phenol S-adenosyl-L-homocysteine + anisole
Thus, the two substrates of this enzyme are S-adenosyl methionine and phenol, whereas its two products are S-adenosylhomocysteine and anisole.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:phenol O-methyltransferase. This enzyme is also called PMT. This enzyme participates in tyrosine metabolism.
References
EC 2.1.1
Enzymes of unknown structure
O-methylated natural phenols metabolism |
https://en.wikipedia.org/wiki/Phosphatidylethanolamine%20N-methyltransferase | Phosphatidylethanolamine N-methyltransferase (abbreviated PEMT) is a transferase enzyme () which converts phosphatidylethanolamine (PE) to phosphatidylcholine (PC) in the liver. In humans it is encoded by the PEMT gene within the Smith–Magenis syndrome region on chromosome 17.
While the CDP-choline pathway, in which choline obtained either by dietary consumption or by metabolism of choline-containing lipids is converted to PC, accounts for approximately 70% of PC biosynthesis in the liver, the PEMT pathway has been shown to have played a critical evolutionary role in providing PC during times of starvation. Furthermore, PC made via PEMT plays a wide range of physiological roles, utilized in choline synthesis, hepatocyte membrane structure, bile secretion, and very low-density lipoprotein (VLDL) secretion.
Nomenclature
Phosphatidylethanolamine N-methyltransferase is also known as lipid methyl transferase, LMTase, phosphatidylethanolamine methyltransferase, phosphatidylethanolamine-N-methylase, and phosphatidylethanolamine-S-adenosylmethionine-methyltransferase.
Function
The PEMT enzyme converts phosphatidylethanolamine (PE) to phosphatidylcholine (PC) via three sequential methylations by S-adenosyl methionine (SAM). The enzyme is found in endoplasmic reticulum and mitochondria-associated membranes. It accounts for ~30% of PC biosynthesis, with the CDP-choline, or Kennedy, pathway making ~70%. PC, typically the most abundant phospholipid in animals and plants, account |
https://en.wikipedia.org/wiki/Phosphatidyl-N-methylethanolamine%20N-methyltransferase | In enzymology, a phosphatidyl-N-methylethanolamine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
Thus, the two substrates of this enzyme are S-adenosyl methionine and phosphatidyl-N-methylethanolamine, whereas its two products are S-adenosylhomocysteine and phosphatidyl-N-dimethylethanolamine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:phosphatidyl-N-methylethanolamine N-methyltransferase. Other names in common use include phosphatidylmonomethylethanolamine methyltransferase, methyltransferase II, phospholipid methyltransferase, PLMT, phosphatidyl-N-methylethanolamine methyltransferase, phosphatidyl-N-monomethylethanolamine methyltransferase, phosphatidylethanolamine methyltransferase I, and phosphatidylmonomethylethanolamine methyltransferase. This enzyme participates in glycine, serine and threonine metabolism and glycerophospholipid metabolism.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoethanolamine%20N-methyltransferase | In enzymology, a phosphoethanolamine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + ethanolamine phosphate S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
Thus, the two substrates of this enzyme are S-adenosyl methionine and ethanolamine phosphate, whereas its two products are S-adenosylhomocysteine and N-methylethanolamine phosphate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:ethanolamine-phosphate N-methyltransferase. This enzyme is also called phosphoethanolamine methyltransferase. This enzyme participates in glycerophospholipid metabolism.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/MMP14 | Matrix metalloproteinase-14 is an enzyme that in humans is encoded by the MMP14 gene.
Function
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Deficits in MMP14 leads to premature aging, short lifespan, and cell senescence in mice, suggesting an important role of MMP14 in extracellular matrix remodeling during aging. Most MMP's are secreted as inactive pro-proteins which are activated when cleaved by extracellular proteinases.
However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are tethered to the cell surface rather than secreted.
"This protein activates MMP2 protein, and this activity may be involved in tumor invasion."
Interactions
MMP14 has been shown to interact with TIMP2.
See also
Matrix metalloproteinase
ARK5
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: M10.014
Matrix metalloproteinases
EC 3.4.24 |
https://en.wikipedia.org/wiki/Polysaccharide%20O-methyltransferase | In enzymology, a polysaccharide O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 1,4-alpha-D-glucooligosaccharide S-adenosyl-L-homocysteine + oligosaccharide containing 6-methyl-D-glucose units
Thus, the two substrates of this enzyme are S-adenosyl methionine and 1,4-alpha-D-glucooligosaccharide, whereas its two products are S-adenosylhomocysteine and oligosaccharide containing 6-methyl-D-glucose units.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:1,4-alpha-D-glucan 6-O-methyltransferase. Other names in common use include polysaccharide methyltransferase, and acylpolysacharide 6-methyltransferase.
References
Gene ontology (GO) codes
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Precorrin-2%20C20-methyltransferase | In enzymology, a precorrin-2 C20-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + precorrin-2 S-adenosyl-L-homocysteine + precorrin-3A
The two substrates of this enzyme are S-adenosyl methionine and precorrin 2 and its two products are S-adenosylhomocysteine and precorrin 3A.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:precorrin-4 C20-methyltransferase and another names in common use is CobI. The enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
Cobalamin biosynthesis
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Precorrin-3B%20C17-methyltransferase | In enzymology, precorrin-3B C17-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + precorrin-3B S-adenosyl-L-homocysteine + precorrin-4
The two substrates of this enzyme are S-adenosyl methionine and precorrin 3B, and its two products are S-adenosylhomocysteine and precorrin 4.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:precorrin-3B C17-methyltransferase. Other names in common use include precorrin-3 methyltransferase, and CobJ. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria and during this step the macrocycle ring-contracts so that the corrin core of the vitamin is formed.
See also
Cobalamin biosynthesis
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Precorrin-4%20C11-methyltransferase | In enzymology, a precorrin-4 C11-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + precorrin-4 S-adenosyl-L-homocysteine + precorrin-5
The two substrates of this enzyme are S-adenosyl methionine and precorrin 4; its two products are S-adenosylhomocysteine and precorrin 5.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:precorrin-4 C11 methyltransferase. Other names in common use include precorrin-3 methylase, and CobM. It is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
Cobalamin biosynthesis
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Precorrin-6A%20synthase%20%28deacetylating%29 | In enzymology, precorrin-6A synthase (deacetylating) () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + precorrin-5 + H2O S-adenosyl-L-homocysteine + precorrin-6A + acetate
The 3 substrates of this enzyme are S-adenosyl methionine, precorrin 5, and H2O. Its 3 products are S-adenosylhomocysteine, precorrin 6A, and acetate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:precorrin-5 C1-methyltransferase (deacetylating). Other names in common use include precorrin-6X synthase (deacetylating), and CobF. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
Cobalamin biosynthesis
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/MAP2K1 | Dual specificity mitogen-activated protein kinase kinase 1 is an enzyme that in humans is encoded by the MAP2K1 gene.
Function
The protein encoded by this gene is a member of the dual-specificity protein kinase family that acts as a mitogen-activated protein (MAP) kinase kinase. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This protein kinase lies upstream of MAP kinases and stimulates the enzymatic activity of MAP kinases upon activation by a wide variety of extra- and intracellular signals. As an essential component of the MAP kinase signal transduction pathway, this kinase is involved in many cellular processes such as proliferation, differentiation, transcription regulation and development. MAP2K1 is altered in 1.05% of all human cancers.
Meiosis
The genomes of diploid organisms in natural populations are highly polymorphic for insertions and deletions. During meiosis double-strand breaks (DSBs) that form within such polymorphic regions must be repaired by inter-sister chromatid exchange, rather than by inter-homolog exchange. Molecular-level studies of recombination during budding yeast meiosis have shown that recombination events initiated by DSBs in regions that lack corresponding sequences in the homolog are efficiently repaired by inter-sister chromatid recombination. This recombination occurs with the same timing as inter-homolog recombination, but with reduced (2- to 3 |
https://en.wikipedia.org/wiki/Precorrin-6Y%20C5%2C15-methyltransferase%20%28decarboxylating%29 | In enzymology, a precorrin-6Y C5,15-methyltransferase (decarboxylating) () is an enzyme that catalyzes the chemical reaction
2 S-adenosyl-L-methionine + precorrin-6Y 2 S-adenosyl-L-homocysteine + precorrin-8X + CO2
The two substrates of this enzyme are S-adenosyl methionine and precorrin 6Y; its three products are S-adenosylhomocysteine, precorrin 8X, and CO2.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:1-precorrin-6Y C5,15-methyltransferase (C-12-decarboxylating). Other names in common use include precorrin-6 methyltransferase, precorrin-6Y methylase and CobL. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
Cobalamin biosynthesis
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Protein-glutamate%20O-methyltransferase | In enzymology, a protein-glutamate O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + protein L-glutamate S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
Thus, the two substrates of this enzyme are S-adenosyl methionine and protein L-glutamic acid, whereas its two products are S-adenosylhomocysteine and protein L-glutamate methyl ester.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:protein-L-glutamate O-methyltransferase. Other names in common use include methyl-accepting chemotaxis protein O-methyltransferase, S-adenosylmethionine-glutamyl methyltransferase, methyl-accepting chemotaxis protein methyltransferase II, S-adenosylmethionine:protein-carboxyl O-methyltransferase, protein methylase II, MCP methyltransferase I, MCP methyltransferase II, protein O-methyltransferase, protein(aspartate)methyltransferase, protein(carboxyl)methyltransferase, protein carboxyl-methylase, protein carboxyl-O-methyltransferase, protein carboxylmethyltransferase II, protein carboxymethylase, protein carboxymethyltransferase, and protein methyltransferase II. This enzyme participates in bacterial chemotaxis - general and bacterial chemotaxis - organism-specific.
CheR proteins are part of the chemotaxis signaling mechanism which methylates the chemotaxis receptor at specific glutamate resid |
https://en.wikipedia.org/wiki/Protein-histidine%20N-methyltransferase | In enzymology, a protein-histidine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + protein L-histidine S-adenosyl-L-homocysteine + protein Ntau-methyl-L-histidine
Thus, the two substrates of this enzyme are S-adenosyl methionine and protein L-histidine, whereas its two products are S-adenosylhomocysteine and protein Ntau-methyl-L-histidine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:protein-L-histidine N-tele-methyltransferase. Other names in common use include protein methylase IV, protein (histidine) methyltransferase, actin-specific histidine methyltransferase, and S-adenosyl methionine:protein-histidine N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/YWHAZ | 14-3-3 protein zeta/delta (14-3-3ζ) is a protein that in humans is encoded by the YWHAZ gene on chromosome 8. The protein encoded by this gene is a member of the 14-3-3 protein family and a central hub protein for many signal transduction pathways. 14-3-3ζ is a major regulator of apoptotic pathways critical to cell survival and plays a key role in a number of cancers and neurodegenerative diseases.
Structure
14-3-3 proteins generally form ~30 kDa-long homo- or heterodimers. Each of the monomers are composed of 9 antiparallel alpha helices. Four alpha-helices (αC, αE, αG, and αI) form an amphipathic groove that serves as the ligand binding site, which can recognize three types of consensus binding motifs: RXX(pS/pT)XP, RXXX(pS/pT)XP, and (pS/pT)X1-2-COOH (where pS/pT represents phosphorylated serine/threonine). In addition to these primary interactions, the target protein can also bind outside the groove via secondary interactions.
In particular, the crystallized structure of 14-3-3ζ forms a cup-shaped dimer when complexed with CBY.
The YWHAZ gene encodes two transcript variants which differ in the 5' UTR but produce the same protein.
Function
14-3-3ζ is one of 7 members of the 14-3-3 protein family, which is ubiquitously expressed and highly conserved among plants and mammals. This protein family is known for regulating signal transduction pathways primarily through binding phosphoserine proteins, though it can also bind phosphothreonine proteins and unphosphorylated prot |
https://en.wikipedia.org/wiki/Protein-S-isoprenylcysteine%20O-methyltransferase | The isoprenylcysteine o-methyltransferase () carries out carboxyl methylation of cleaved eukaryotic proteins that terminate in a CaaX motif. In Saccharomyces cerevisiae (Baker's yeast) this methylation is carried out by Ste14p, an integral endoplasmic reticulum membrane protein. Ste14p is the founding member of the isoprenylcysteine carboxyl methyltransferase (ICMT) family, whose members share significant sequence homology.
The enzyme catalyzes the chemical reaction
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester
Thus, the two substrates of this enzyme are S-adenosyl methionine and protein C-terminal S-farnesyl-L-cysteine, whereas its two products are S-adenosylhomocysteine and protein C-terminal S-farnesyl-L-cysteine methyl ester.
References
EC 2.1.1
Enzymes of known structure
Protein families
Transmembrane proteins |
https://en.wikipedia.org/wiki/Putrescine%20N-methyltransferase | In enzymology, a putrescine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + putrescine S-adenosyl-L-homocysteine + N-methylputrescine
Thus, the two substrates of this enzyme are S-adenosyl methionine and putrescine, whereas its two products are S-adenosylhomocysteine and N-methylputrescine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:putrescine N-methyltransferase. This enzyme is also called putrescine methyltransferase. This enzyme participates in alkaloid biosynthesis ii.
This enzyme is important in the synthesis of many plant alkaloids. It evolved from spermidine synthase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyridine%20N-methyltransferase | In enzymology, a pyridine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + pyridine S-adenosyl-L-homocysteine + N-methylpyridinium
Thus, the two substrates of this enzyme are S-adenosyl methionine and pyridine, whereas its two products are S-adenosylhomocysteine and N-methylpyridinium.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:pyridine N-methyltransferase. This enzyme is also called pyridine methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Quercetin%203-O-methyltransferase | In enzymology, a quercetin 3-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3,5,7,3',4'-pentahydroxyflavone S-adenosyl-L-homocysteine + 3-methoxy-5,7,3',4'-tetrahydroxyflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3,5,7,3',4'-pentahydroxyflavone, whereas its two products are S-adenosylhomocysteine and 3-methoxy-5,7,3',4'-tetrahydroxyflavone.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3,5,7,3',4'-pentahydroxyflavone 3-O-methyltransferase. Other names in common use include flavonol 3-O-methyltransferase, and flavonoid 3-methyltransferase. This enzyme participates in flavonoid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure
Quercetin
Flavonols metabolism
O-methylated flavonoids metabolism |
https://en.wikipedia.org/wiki/%28Ribulose-bisphosphate%20carboxylase%29-lysine%20N-methyltransferase | In enzymology, a [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N-methyl-L-lysine
Thus, the two substrates of this enzyme are S-adenosyl methionine and ribulose-1,5-bisphosphate carboxylase-lysine, whereas its two products are S-adenosylhomocysteine and ribulose-1,5-bisphosphate carboxylase-N6-methyl-L-lysine.
Transferase Family
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases.
The systematic name of this enzyme class is S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine N6-methyltransferase.
Other names in common use include rubisco methyltransferase, ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, epsilonN-methyltransferase, S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase, and (dimerizing)]-lysine 6-N-methyltransferase.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/RRNA%20%28adenine-N6-%29-methyltransferase | In enzymology, a rRNA (adenine-N6-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + rRNA S-adenosyl-L-homocysteine + rRNA containing N6-methyladenine
Thus, the two substrates of this enzyme are S-adenosyl methionine and rRNA, whereas its two products are S-adenosylhomocysteine and rRNA containing N6-methyladenine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:rRNA (adenine-N6-)-methyltransferase. Other names in common use include ribosomal ribonucleate adenine 6-methyltransferase, gene ksgA methyltransferase, ribonucleic acid-adenine (N6) methylase, ErmC 23S rRNA methyltransferase, and S-adenosyl-L-methionine:rRNA (adenine-6-N-)-methyltransferase.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/RRNA%20%28guanine-N1-%29-methyltransferase | In enzymology, a rRNA (guanine-N1-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + rRNA S-adenosyl-L-homocysteine + rRNA containing N1-methylguanine
Thus, the two substrates of this enzyme are S-adenosyl methionine and rRNA, whereas its two products are S-adenosylhomocysteine and rRNA containing N1-methylguanine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:rRNA (guanine-N1-)-methyltransferase. Other names in common use include ribosomal ribonucleate guanine 1-methyltransferase, and S-adenosyl-L-methionine:rRNA (guanine-1-N-)-methyltransferase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/RRNA%20%28guanine-N2-%29-methyltransferase | In enzymology, a rRNA (guanine-N2-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + rRNA S-adenosyl-L-homocysteine + rRNA containing N2-methylguanine
Thus, the two substrates of this enzyme are S-adenosyl methionine and rRNA, whereas its two products are S-adenosylhomocysteine and rRNA containing N2-methylguanine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:rRNA (guanine-N2-)-methyltransferase. Other names in common use include ribosomal ribonucleate guanine-2-methyltransferase, and S-adenosyl-L-methionine:rRNA (guanine-2-N-)-methyltransferase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28RS%29-1-benzyl-1%2C2%2C3%2C4-tetrahydroisoquinoline%20N-methyltransferase | In enzymology, a (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase is an enzyme that catalyzes the chemical reaction:
S-adenosyl-L-methionine + (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline S-adenosyl-L-homocysteine + N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline
This enzyme participates in alkaloid biosynthesis.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase. This enzyme is also called norreticuline N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28RS%29-norcoclaurine%206-O-methyltransferase | In enzymology, a (RS)-norcoclaurine 6-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + (RS)-norcoclaurine S-adenosyl-L-homocysteine + (RS)-coclaurine
Thus, the two substrates of this enzyme are S-adenosyl methionine and (R,S)-norcoclaurine, whereas its two products are S-adenosylhomocysteine and (R,S)-coclaurine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(RS)-norcoclaurine 6-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-coclaurine-N-methyltransferase | In enzymology, a (S)-coclaurine-N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + (S)-coclaurine S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
Thus, the two substrates of this enzyme are S-adenosyl methionine and (S)-coclaurine, whereas its two products are S-adenosylhomocysteine and (S)-N-methylcoclaurine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(S)-coclaurine-N-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-scoulerine%209-O-methyltransferase | In enzymology, a (S)-scoulerine 9-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + (S)-scoulerine S-adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
Thus, the two substrates of this enzyme are S-adenosyl methionine and (S)-scoulerine, whereas its two products are S-adenosylhomocysteine and (S)-tetrahydrocolumbamine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(S)-scoulerine 9-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sterigmatocystin%208-O-methyltransferase | In enzymology, a sterigmatocystin 8-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + sterigmatocystin S-adenosyl-L-homocysteine + 8-O-methylsterigmatocystin
Thus, the two substrates of this enzyme are S-adenosyl methionine and sterigmatocystin, whereas its two products are S-adenosylhomocysteine and 8-O-methylsterigmatocystin.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:sterigmatocystin 8-O-methyltransferase. Other names in common use include sterigmatocystin methyltransferase, O-methyltransferase II, sterigmatocystin 7-O-methyltransferase (incorrect), S-adenosyl-L-methionine:sterigmatocystin 7-O-methyltransferase, and (incorrect).
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sterol%2024-C-methyltransferase | In enzymology, a sterol 24-C-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5alpha-cholesta-8,24-dien-3beta-ol, whereas its two products are S-adenosylhomocysteine and 24-methylene-5alpha-cholest-8-en-3beta-ol.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:zymosterol 24-C-methyltransferase. Other names in common use include Delta24-methyltransferase, Delta24-sterol methyltransferase, zymosterol-24-methyltransferase, S-adenosyl-4-methionine:sterol Delta24-methyltransferase, SMT1, 24-sterol C-methyltransferase, S-adenosyl-L-methionine:Delta24(23)-sterol methyltransferase, and phytosterol methyltransferase. This enzyme participates in biosynthesis of steroids. It employs one cofactor, glutathione.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-tetrahydroprotoberberine%20N-methyltransferase | In enzymology, a (S)-tetrahydroprotoberberine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + (S)-7,8,13,14-tetrahydroprotoberberine S-adenosyl-L-homocysteine + cis-N-methyl-(S)-7,8,13,14-tetrahydroprotoberberine
Thus, the two substrates of this enzyme are S-adenosyl methionine and (S)-7,8,13,14-tetrahydroprotoberberine, whereas its two products are S-adenosylhomocysteine and cis-N-methyl-(S)-7,8,13,14-tetrahydroprotoberberine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(S)-7,8,13,14-tetrahydroprotoberberine cis-N-methyltransferase. This enzyme is also called tetrahydroprotoberberine cis-N-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tabersonine%2016-O-methyltransferase | In enzymology, a tabersonine 16-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 16-hydroxytabersonine S-adenosyl-L-homocysteine + 16-methoxytabersonine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 16-hydroxytabersonine, whereas its two products are S-adenosylhomocysteine and 16-methoxytabersonine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:16-hydroxytabersonine 16-O-methyltransferase. Other names in common use include 11-demethyl-17-deacetylvindoline 11-methyltransferase, 11-O-demethyl-17-O-deacetylvindoline O-methyltransferase, S-adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline, and 11-O-methyltransferase. This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tetrahydrocolumbamine%202-O-methyltransferase | In enzymology, a tetrahydrocolumbamine 2-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 5,8,13,13a-tetrahydrocolumbamine S-adenosyl-L-homocysteine + tetrahydropalmatine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5,8,13,13a-tetrahydrocolumbamine, whereas its two products are S-adenosylhomocysteine and tetrahydropalmatine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:5,8,13,13a-tetrahydrocolumbamine 2-O-methyltransferase. This enzyme is also called tetrahydrocolumbamine methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tetrahydromethanopterin%20S-methyltransferase | In enzymology, a tetrahydromethanopterin S-methyltransferase () is an enzyme that catalyzes the chemical reaction
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate 5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
Thus, the two substrates of this enzyme are 5-methyl-5,6,7,8-tetrahydromethanopterin and 2-mercaptoethanesulfonate (coenzyme M), whereas its two products are 5,6,7,8-tetrahydromethanopterin and 2-(methylthio)ethanesulfonate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5-methyl-5,6,7,8-tetrahydromethanopterin:2-mercaptoethanesulfonate 2-methyltransferase. This enzyme is also called tetrahydromethanopterin methyltransferase. This enzyme participates in folate biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Theobromine%20synthase | In enzymology, a theobromine synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 7-methylxanthine S-adenosyl-L-homocysteine + 3,7-dimethylxanthine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 7-methylxanthine, whereas its two products are S-adenosylhomocysteine and 3,7-dimethylxanthine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:7-methylxanthine N3-methyltransferase. Other names in common use include monomethylxanthine methyltransferase, MXMT, CTS1, CTS2, and S-adenosyl-L-methionine:7-methylxanthine 3-N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thetin%E2%80%94homocysteine%20S-methyltransferase | In enzymology, a thetin-homocysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
dimethylsulfonioacetate + L-homocysteine S-methylthioglycolate + L-methionine
Thus, the two substrates of this enzyme are dimethylsulfonioacetic acid and L-homocysteine, whereas its two products are S-methylthioglycolic acid and L-methionine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is dimethylsulfonioacetic acid:L-homocysteine S-methyltransferase. Other names in common use include dimethylthetin-homocysteine methyltransferase, and thetin-homocysteine methylpherase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thioether%20S-methyltransferase | In enzymology, a thioether S-methyltransferase () is an enzyme that catalyzes the chemical reaction.
S-adenosyl-L-methionine + dimethyl sulfide S-adenosyl-L-homocysteine + trimethylsulfonium
Thus, the two substrates of this enzyme are S-adenosyl methionine and dimethyl sulfide, whereas its two products are S-adenosylhomocysteine and trimethylsulfonium.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:dimethyl-sulfide S-methyltransferase. Other names in common use include S-adenosyl-L-methionine:thioether S-methyltransferase, and thioether methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiol%20S-methyltransferase | In enzymology, a thiol S-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + a thiol S-adenosyl-L-homocysteine + a thioether
Thus, the two substrates of this enzyme are S-adenosyl methionine and thiol, whereas its two products are S-adenosylhomocysteine and thioether.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:thiol S-methyltransferase. Other names in common use include S-methyltransferase, thiol methyltransferase, and TMT. This enzyme participates in selenoamino acid metabolism.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thymidylate%20synthase%20%28FAD%29 | In enzymology, a thymidylate synthase (FAD) () is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydrofolate + dUMP + FADH2 dTMP + tetrahydrofolate + FAD
The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, dUMP, and FADH2, whereas its 3 products are dTMP, tetrahydrofolate, and FAD.
This enzyme belongs to the family of transferases, to be specific those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate,FADH2:dUMP C-methyltransferase. Other names in common use include Thy1, and ThyX. This enzyme participates in pyrimidine metabolism and one carbon pool by folate.
Most organisms, including humans, use the thyA- or TYMS-encoded classic thymidylate synthase whereas some bacteria use the similar flavin-dependent thymidylate synthase (FDTS) instead.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
See also
Thymidylate synthetase
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tocopherol%20O-methyltransferase | In enzymology, a tocopherol O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + gamma-tocopherol S-adenosyl-L-homocysteine + alpha-tocopherol
Thus, the two substrates of this enzyme are S-adenosyl methionine and gamma-tocopherol, whereas its two products are S-adenosylhomocysteine and alpha-tocopherol.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:gamma-tocopherol 5-O-methyltransferase. This enzyme is also called gamma-tocopherol methyltransferase. This enzyme participates in biosynthesis of steroids.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trans-aconitate%202-methyltransferase | In enzymology, a trans-aconitate 2-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + trans-aconitate S-adenosyl-L-homocysteine + (E)-3-(methoxycarbonyl)pent-2-enedioate
Thus, the two substrates of this enzyme are S-adenosyl methionine and trans-aconitate, whereas its two products are S-adenosylhomocysteine and (E)-3-(methoxycarbonyl)pent-2-enedioate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 2'-O-methyltransferase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Trans-aconitate%203-methyltransferase | In enzymology, a trans-aconitate 3-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + trans-aconitate S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate
Thus, the two substrates of this enzyme are S-adenosyl methionine and trans-aconitate, whereas its two products are S-adenosylhomocysteine and (E)-2-(methoxycarbonylmethyl)butenedioate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 3'-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trimethylsulfonium%E2%80%94tetrahydrofolate%20N-methyltransferase | In enzymology, a trimethylsulfonium-tetrahydrofolate N-methyltransferase () is an enzyme that catalyzes the chemical reaction
trimethylsulfonium + tetrahydrofolate dimethylsulfide + 5-methyltetrahydrofolate
Thus, the two substrates of this enzyme are trimethylsulfonium and tetrahydrofolate, whereas its two products are dimethyl sulfide and 5-methyltetrahydrofolate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is trimethylsulfonium:tetrahydrofolate N-methyltransferase. This enzyme is also called trimethylsulfonium-tetrahydrofolate methyltransferase. This enzyme participates in one carbon pool by folate.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/TRNA%20%285-methylaminomethyl-2-thiouridylate%29-methyltransferase | In enzymology, a tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing 5-methylaminomethyl-2-thiouridylic acid.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (5-methylaminomethyl-2-thio-uridylate)-methyltransferase. Other names in common use include transfer ribonucleate 5-methylaminomethyl-2-thiouridylate, 5-methyltransferase, and tRNA 5-methylaminomethyl-2-thiouridylate 5'-methyltransferase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA%20%28adenine-N1-%29-methyltransferase | In enzymology, a tRNA (adenine-N1-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N1-methyladenine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N1-methyladenine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (adenine-N1-)-methyltransferase. Other names in common use include transfer ribonucleate adenine 1-methyltransferase, transfer RNA (adenine-1) methyltransferase, 1-methyladenine transfer RNA methyltransferase, adenine-1-methylase, and S-adenosyl-L-methionine:tRNA (adenine-1-N-)-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Bipolar%20transistor%20biasing | Bipolar transistors must be properly biased to operate correctly. In circuits made with individual devices (discrete circuits), biasing networks consisting of resistors are commonly employed. Much more elaborate biasing arrangements are used in integrated circuits, for example, bandgap voltage references and current mirrors. The voltage divider configuration achieves the correct voltages by the use of resistors in certain patterns. By selecting the proper resistor values, stable current levels can be achieved that vary only little over temperature and with transistor properties such as β.
The operating point of a device, also known as bias point, quiescent point, or Q-point, is the point on the output characteristics that shows the DC collector–emitter voltage (Vce) and the collector current (Ic) with no input signal applied.
Bias circuit requirements
A bias network is selected to stabilize the operating point of the transistor, by reducing the following effects of device variability, temperature, and voltage changes:
The gain of a transistor can vary significantly between different batches, which results in widely different operating points for sequential units in serial production or after replacement of a transistor.
Due to the Early effect, the current gain is affected by the collector–emitter voltage.
Both gain and base–emitter voltage depend on the temperature.
The leakage current also increases with temperature.
A bias circuit may be composed of only resistors |
https://en.wikipedia.org/wiki/TRNA%20%28adenine-N6-%29-methyltransferase | In enzymology, a tRNA (adenine-N6-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N6-methyladenine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N6-methyladenine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (adenine-N6-)-methyltransferase. This enzyme is also called S-adenosyl-L-methionine:tRNA (adenine-6-N-)-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/TRNA%20%28cytosine-5-%29-methyltransferase | In enzymology, a tRNA (cytosine-5-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing 5-methylcytosine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing 5-methylcytosine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (cytosine-5-)-methyltransferase. Other names in common use include transfer ribonucleate cytosine 5-methyltransferase, and transfer RNA cytosine 5-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/TRNA%20%28guanine-N1-%29-methyltransferase | In enzymology, a tRNA (guanine-N1-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N1-methylguanine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (guanine-N1-)-methyltransferase. Other names in common use include transfer ribonucleate guanine 1-methyltransferase, tRNA guanine 1-methyltransferase, and S-adenosyl-L-methionine:tRNA (guanine-1-N-)-methyltransferase.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA%20%28guanine-N2-%29-methyltransferase | In enzymology, a tRNA (guanine-N2-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N2-methylguanine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N2-Methylguanine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (guanine-N2-)-methyltransferase. Other names in common use include transfer ribonucleate guanine 2-methyltransferase, transfer ribonucleate guanine N2-methyltransferase, transfer RNA guanine 2-methyltransferase, guanine-N2-methylase, and S-adenosyl-L-methionine:tRNA (guanine-2-N-)-methyltransferase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA%20%28guanine-N7-%29-methyltransferase | In enzymology, a tRNA (guanine-N7-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N7-methylguanine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (guanine-N7-)-methyltransferase. Other names in common use include transfer ribonucleate guanine 7-methyltransferase, 7-methylguanine transfer ribonucleate methylase, tRNA guanine 7-methyltransferase, N7-methylguanine methylase, and S-adenosyl-L-methionine:tRNA (guanine-7-N-)-methyltransferase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA%20guanosine-2%27-O-methyltransferase | In enzymology, a tRNA guanosine-2'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanosine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing 2'-O-methylguanosine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA guanosine-2'-O-methyltransferase. Other names in common use include transfer ribonucleate guanosine 2'-methyltransferase, tRNA guanosine 2'-methyltransferase, tRNA (guanosine 2')-methyltransferase, tRNA (Gm18) 2'-O-methyltransferase, tRNA (Gm18) methyltransferase, tRNA (guanosine-2'-O-)-methyltransferase, and S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA%20%28uracil-5-%29-methyltransferase | In enzymology, a tRNA (uracil-5-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA containing uridine at position 54 S-adenosyl-L-homocysteine + tRNA containing ribothymidine at position 54
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA containing uridine at position 54, whereas its two products are S-adenosylhomocysteine and tRNA containing ribothymidine at position 54.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (uracil-5-)-methyltransferase. Other names in common use include ribothymidyl synthase, transfer RNA uracil 5-methyltransferase, transfer RNA uracil methylase, tRNA uracil 5-methyltransferase, m5U-methyltransferase, tRNA:m5U54-methyltransferase, and RUMT.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CSNK2A2 | Casein kinase II subunit alpha' is an enzyme that in humans is encoded by the CSNK2A2 gene.
Interactions
CSNK2A2 has been shown to interact with over 160 different substrates.
CSNK2A2 has been shown to interact with:
Activating transcription factor 2,
ATF1,
C-Fos,
CREB binding protein,
CSNK2B,
FGF1,
Nucleolin,
PIN1,
PTEN, and
RELA.
References
External links
Further reading |
https://en.wikipedia.org/wiki/Tryptophan%202-C-methyltransferase | In enzymology, a tryptophan 2-C-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + L-tryptophan S-adenosyl-L-homocysteine + L-2-methyltryptophan
Thus, the two substrates of this enzyme are S-adenosyl methionine and L-tryptophan, whereas its two products are S-adenosylhomocysteine and L-2-methyltryptophan.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:L-tryptophan 2-C-methyltransferase. Other names in common use include tryptophan 2-methyltransferase, and S-adenosylmethionine:tryptophan 2-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tyramine%20N-methyltransferase | In enzymology, a tyramine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tyramine S-adenosyl-L-homocysteine + N-methyltyramine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tyramine, whereas its two products are S-adenosylhomocysteine and N-methyltyramine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tyramine N-methyltransferase. Other names in common use include DIB O-methyltransferase (3,5-diiodo-4-hydroxy-benzoic acid), S-adenosyl-methionine:tyramine N-methyltransferase, and tyramine methylpherase. This enzyme participates in tyrosine metabolism.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vitexin%202%22-O-rhamnoside%207-O-methyltransferase | In enzymology, a vitexin 2"-O-rhamnoside 7-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + vitexin 2"-O-beta-L-rhamnoside S-adenosyl-L-homocysteine + 7-O-methylvitexin 2"-O-beta-L-rhamnoside
Thus, the two substrates of this enzyme are S-adenosyl methionine and vitexin 2"-O-beta-L-rhamnoside, whereas its two products are S-adenosylhomocysteine and 7-O-methylvitexin 2"-O-beta-L-rhamnoside.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:vitexin-2"-O-beta-L-rhamnoside 7-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure
O-methylated flavones metabolism |
https://en.wikipedia.org/wiki/G%20protein-coupled%20bile%20acid%20receptor | The G protein-coupled bile acid receptor 1 (GPBAR1) also known G-protein coupled receptor 19 (GPCR19), membrane-type receptor for bile acids (M-BAR) or TGR5 as is a protein that in humans is encoded by the GPBAR1 gene.
Function
This gene encodes a member of the G protein-coupled receptor (GPCR) superfamily. This protein functions as a cell surface receptor for bile acids. Treatment of cells expressing this GPCR with bile acids induces the production of intracellular cAMP, activation of a MAP kinase signaling pathway, and internalization of the receptor. The receptor is implicated in the suppression of macrophage functions and regulation of energy homeostasis by bile acids.
One effect of this receptor is to activate deiodinases which convert the prohormone thyroxine (T4) to the active hormone triiodothyronine (T3). T3 in turn activates the thyroid hormone receptor which increases metabolic rate.
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Cyclin%20T1 | Cyclin-T1 is a protein that in humans is encoded by the CCNT1 gene.
Function
The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns that contribute to the temporal coordination of each mitotic event. This cyclin tightly associates with CDK9 kinase, and was found to be a major subunit of the transcription elongation factor p-TEFb. The kinase complex containing this cyclin and the elongation factor can interact with, and act as a cofactor of human immunodeficiency virus type 1 (HIV-1) Tat protein, and was shown to be both necessary and sufficient for full activation of viral transcription. This cyclin and its kinase partner were also found to be involved in the phosphorylation and regulation of the carboxy-terminal domain (CTD) of the largest RNA polymerase II subunit.
Interactions
Cyclin T1 has been shown to interact with the following:
Aryl hydrocarbon receptor
CDK9
Granulin
HEXIM1
Myc
NUFIP1
Promyelocytic leukemia protein
References
Further reading |
https://en.wikipedia.org/wiki/NFKB2 | Nuclear factor NF-kappa-B p100 subunit is a protein that in humans is encoded by the NFKB2 gene.
Function
NF-κB has been detected in numerous cell types that express cytokines, chemokines, growth factors, cell adhesion molecules, and some acute phase proteins in health and in various disease states. NF-κB is activated by a wide variety of stimuli such as cytokines, oxidant-free radicals, inhaled particles, ultraviolet irradiation, and bacterial or viral products. Inappropriate activation of NF-kappa-B has been linked to inflammatory events associated with autoimmune arthritis, asthma, septic shock, lung fibrosis, glomerulonephritis, atherosclerosis, and AIDS. In contrast, complete and persistent inhibition of NF-kappa-B has been linked directly to apoptosis, inappropriate immune cell development, and delayed cell growth. For reviews, see Chen et al. (1999) and Baldwin (1996).[supplied by OMIM]
Clinical significance
Mutation of the NFKB2 gene has been linked to Common variable immunodeficiency (CVID) as the cause of the disease. Other genes might also be responsible. The frequency of NFKB2 mutation in CVID population is yet to be established.
The protein NFKB2 can become mutated and lead to hereditary endocrine and immuneodeficiences. The mutation occurs at the C-terminus of NFKB2 and it causes common variable immunodeficienciency which in turn causes endocrine deficiency and immunodeficiencies. A NFKB2 mutation can cause things like adrenocorticotropic hormone deficien |
https://en.wikipedia.org/wiki/Phosphatidylinositol%20transfer%20protein | Phosphatidylinositol transfer protein (PITP) or priming in exocytosis protein 3 (PEP3) is a ubiquitous cytosolic domain involved in transport of phospholipids from their site of synthesis in the endoplasmic reticulum and Golgi to other
cell membranes.
Biological function
PITP has been also shown to be an essential component of the polyphosphoinositide synthesis machinery and is hence required for proper signalling by epidermal growth factor and f-Met-Leu-Phe, as well as for exocytosis. The role of PITP in polyphosphoinositide synthesis may also explain its involvement in intracellular vesicular traffic.
Structure and evolution
Along with the structurally unrelated Sec14p family (found in ), this family can bind/exchange one molecule of phosphatidylinositol (PI) or phosphatidylcholine (PC) and thus aids their transfer between different membrane compartments. There are three sub-families - all share an N-terminal PITP-like domain, whose sequence is highly conserved. It is described as consisting of three regions. The N-terminal region is thought to bind the lipid and contains two helices and an eight-stranded, mostly antiparallel beta-sheet. An intervening loop region, which is thought to play a role in protein-protein interactions, separates this from the C-terminal region, which exhibits the greatest sequence variation and may be involved in membrane binding. This motif marks PITP as part of the larger SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) domain superfamily.
PIT |
https://en.wikipedia.org/wiki/Interstitial%20collagenase | Interstitial collagenase, also known as fibroblast collagenase, and matrix metalloproteinase-1 (MMP-1) is an enzyme that in humans is encoded by the MMP1 gene. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP-1 was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA. MMP-1 has an estimated molecular mass of 54 kDa.
Structure
MMP-1 has an archetypal structure consisting of a pre-domain, a pro-domain, a catalytic domain, a linker region and a hemopexin-like domain. The primary structure of MMP-1 was first published by Goldberg, G I, et al. Two main nomenclatures for the primary structure are currently in use, the original one from which the first amino-acid starts with the signalling peptide and a second one where the first amino-acid starts counting from the prodomain (proenzyme nomenclature).
Catalytic domain
The catalytic domains of MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40 Å. Despite the similarity of the catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 catalytic domain.
Overall structural characteristics
The catalytic domain of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role.
The catalytic domain (CAT) of MMP-1 starts with t |
https://en.wikipedia.org/wiki/Nagy%20Habib | Nagy Habib (born 1952), is professor of hepato-biliary surgery at Imperial College, London, and is known for devising radio-frequency based liver resection devices which remove liver tumour with minimal blood loss. His work has also focused on stem cells and gene therapy.
Early life and education
Nagy Habib was born in Cairo, Egypt, 1952. He trained under both and the transplant surgeon Thomas Starzl.
Career
His work has focused on stem cells and gene therapy. He led the first clinical trial in the use of oncolytic adenoviruses for the treatment of liver cancer. It was carried out by means of a locally restricted injection into the main blood vessel to the liver. The findings were published in 2001. It was found to be safe, but the second phase of the trial did not find it effective. In 2004, he took stem cells from a person with liver cirrhosis and injected them into their liver artery, resulting in some improvement of liver function.
In 2003 he was appointed professor of hepato-biliary surgery at Imperial College, London. In June 2007 he was appointed pro-rector for Commercial Affairs at Imperial.
Habib developed several radio-frequency (RF) based liver resection devices. He devised the Habib RF device using the Habib needle, which has a modified version called the Habib 4X. It removes tumour with minimal blood loss. The procedure has come to be known as 'Habib's resection'.
MiNA Therapeutics, a biotechnology company dealing in small activating RNA technology was co-f |
https://en.wikipedia.org/wiki/Glutathione%20S-transferase%20Mu%201 | Glutathione S-transferase Mu 1 (gene name GSTM1) is a human glutathione S-transferase.
Function
Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a cytoplasmic glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress, by conjugation with glutathione.
The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3, and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins, as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with an increase in a number of cancers, likely due to an increased susceptibility to environmental toxins and carcinogens. Multiple protein isoforms are encoded by transcript variants of this gene.
See also
Biliary atresia
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Glutathione S-transferase Mu 1 |
https://en.wikipedia.org/wiki/GSTP1 | Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene.
Function
Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into four main classes: alpha, mu, pi, and theta. The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.
Interactions
GSTP1 has been shown to interact with Fanconi anemia, complementation group C and MAPK8.
GST-Pi is expressed in many human tissues, particularly in the biliary tree, renal distal convoluted tubules and lungs.
Possible drug target
Triple-negative breast cancer cells rely on glutathione-S-transferase Pi1, and inhibitors are being studied. Piperlongumine has been found to silence the gene.
References
Further reading |
https://en.wikipedia.org/wiki/PTPN6 | Tyrosine-protein phosphatase non-receptor type 6, also known as Src homology region 2 domain-containing phosphatase-1 (SHP-1), is an enzyme that in humans is encoded by the PTPN6 gene.
Function
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling, (e.g., the LYN-CD22-SHP-1 pathway). Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported.
Expression
SHP-1 gene has two promoters: P-1, active in epithelial cells, and P-2, active in hemopoietic cells. In addition the expression of SHP-1 is low in epithelial cells and high in hemopoietic cells. SHP-1 level in epithelial cells increases and in hematopoietic cells decreases in cancer.
Interactions
PTPN6 has been shown to interact with:
BCR gene,
CD117,
CD22,
CD31,
CTNND1,
EGFR,
E |
https://en.wikipedia.org/wiki/Centre%20for%20Artificial%20Intelligence%20and%20Robotics | The Centre for Artificial Intelligence and Robotics (CAIR) is a laboratory of the Defence Research & Development Organization (DRDO). Located in Bangalore, Karnataka, involved in the Research & Development of high quality Secure Communication, Command and Control, and Intelligent Systems. CAIR was founded by Arogyaswami Paulraj. CAIR is the primary laboratory for R&D in different areas of Defence Information and Communication Technology (ICT).
History
CAIR was established in October 1986. Its research focus was initially in the areas of Artificial Intelligence (AI), Robotics, and Control systems. In November 2000, R&D groups working in the areas of Command, Control, Communications & Intelligence (C3I) systems, Communication and Networking, and communication secrecy in Electronics and Radar Development Establishment (LRDE) were merged with CAIR.
CAIR, which was operating from different campuses across Bangalore has now moved .
Projects
DRDO NETRA, software to intercept online communications.
SecOS, Secure Operating System
Muntra - unmanned ground vehicle manufactured at the Ordnance Factory Medak.
External links
CAIR Home Page
Robot soldiers!
Defence Research and Development Organisation laboratories
Artificial intelligence laboratories
Research institutes in Bangalore
Laboratories in India
1986 establishments in Karnataka
Research institutes established in 1986
Robotics in India |
https://en.wikipedia.org/wiki/Samsung%20U740%20Alias | The Samsung Alias (formerly known as the SCH-u740) was a cell phone made by Samsung. The phone was originally available in a champagne finish then black, with the dialing keys in grey in contrast to black keys. A subsequent relaunch under the "Alias" name was accompanied by the switch to a blue/silver color scheme with the dialing keys half white and half black instead of grey and black. It features a dual-hinge design that can be opened portrait or landscape style. In landscape mode it features a QWERTY keyboard and VCAST music on the Verizon Wireless network within Australia and the USA.
The phone runs on Verizon Wireless's digital and Ev-DO networks. It also is available within Canada on Bell Mobility's network.
The music format is WMA. Its external features are a small postage stamp sized front display, touch sensitive music control buttons and a 1.3-megapixel camera with flash. On the right side there is a speakerphone button and a microSD (Transflash) card slot. On the left, there is a hold button along with an up/down volume button and proprietary charger/data transfer port. Opened in portrait mode, a standard numerical dialing pad along with two soft keys, send and end keys, a camera button, a voice command button, and a circular four-point dial with an OK key in the center are all available. Opened horizontally, the full QWERTY keypad is usable and a simple button press allows switching between the various alphanumeric functions. A pair of stereo speakers are mount |
https://en.wikipedia.org/wiki/CBL%20%28gene%29 | Cbl (named after Casitas B-lineage Lymphoma) is a mammalian gene encoding the protein CBL which is an E3 ubiquitin-protein ligase involved in cell signalling and protein ubiquitination. Mutations to this gene have been implicated in a number of human cancers, particularly acute myeloid leukaemia.
Discovery
In 1989 a virally encoded portion of the chromosomal mouse Cbl gene was the first member of the Cbl family to be discovered and was named v-Cbl to distinguish it from normal mouse c-Cbl. The virus used in the experiment was a mouse-tropic strain of Murine leukemia virus isolated from the brain of a mouse captured at Lake Casitas, California known as Cas-Br-M, and was found to have excised approximately a third of the original c-Cbl gene from a mouse into which it was injected. Sequencing revealed that the portion carried by the retrovirus encoded a tyrosine kinase binding domain, and that this was the oncogenic form as retroviruses carrying full-length c-Cbl did not induce tumor formation. The resultant transformed retrovirus was found to consistently induce a type of pre-B lymphoma, known as Casitas B-lineage lymphoma, in infected mice.
Structure
Full length c-Cbl has been found to consist of several regions encoding for functionally distinct protein domains:
N-terminal tyrosine kinase binding domain (TKB domain): determines the protein which it can bind to
RING finger domain motif: recruits enzymes involved in ubiquitination
Proline-rich region: the site of interac |
https://en.wikipedia.org/wiki/Sameridine | Sameridine is a 4-phenylpiperidine derivative that is related to the opioid analgesic drug pethidine (meperidine).
Sameridine has an unusual pharmacological profile, being both a local anaesthetic and a μ-opioid partial agonist. It is currently under development for use in surgical anasthesia, mainly administered by intrathecal infusion. It produces less respiratory depression than morphine, even at a high dose, and produces no respiratory depression at a low dose.
Sameridine is not currently a controlled drug, although if approved for medical use it will certainly be a prescription medicine, and it would probably be assigned to one of the controlled drug schedules in more restrictive jurisdictions such as Australia and the United States, especially if it were found to be addictive in animals.
References
External links
Substituted 4-phenyl-4-piperidinecarboxamides with both local anaesthetic and analgesic effect. US Patent 5227389
Process for the preparation of Sameridine. US Patent 5756748
4-Phenylpiperidines
Synthetic opioids
Carboxamides
Mu-opioid receptor agonists |
https://en.wikipedia.org/wiki/Semorphone | Semorphone (Mr 2264) is an opiate analogue that is an N-substituted derivative of oxymorphone.
Semorphone is a partial agonist at μ-opioid receptors. It is around twice the potency of morphine, but with a ceiling effect on both analgesia and respiratory depression which means that these effects stop becoming any stronger after a certain maximum dose.
It is not currently used in medicine, and is not a controlled drug, although it might be considered to be a controlled substance analogue of oxymorphone on the grounds of its related chemical structure in some jurisdictions such as the United States, Canada, Australia and New Zealand.
References
4,5-Epoxymorphinans
Opioids
Phenols
Tertiary alcohols
Ketones
Ethers
Mu-opioid receptor agonists |
https://en.wikipedia.org/wiki/Signet%20ring%20cell | In histology, a signet ring cell is a cell with a large vacuole. The malignant type is seen predominantly in carcinomas.
Signet ring cells are most frequently associated with stomach cancer, but can arise from any number of tissues including the prostate, bladder, gallbladder, breast, colon, ovarian stroma and testis.
Types
The NCI Thesaurus identifies the following types of signet ring cell
Castration cell, a non-malignant cell arising in the anterior pituitary gland under certain abnormal hormonal conditions.
Neoplastic thyroid gland follicular signet ring cell
Signet ring adenocarcinoma cell
Signet ring melanoma cell
Signet ring stromal cell
Appearance
The name of the cell comes from its appearance; signet ring cells resemble signet rings. They contain a large amount of mucin, which pushes the nucleus to the cell periphery. The pool of mucin in a signet ring cell mimics the appearance of a finger hole and the nucleus mimics the appearance of the face of the ring in profile.
Diagnostic significance
A significant number of signet ring cells, generally, are associated with a worse prognosis.
Classification of carcinomas
SRC carcinomas can be classified using immunohistochemistry.
See also
Signet ring cell carcinoma
References
External links
Signet ring cells - med.Utah.edu.
Signet ring cell definition - cancer.gov.
Signet ring cell cancer information - sites.google.com/site/signetringcancer.
Histopathology |
https://en.wikipedia.org/wiki/Juan%20Antonio | Juan Ignacio Antonio (born 5 January 1988) is an Argentine former professional football who played as a forward.
External links
Argentine Primera statistics
Player profile on the River Plate website
1988 births
Living people
People from Trelew
Footballers from Chubut Province
Argentine men's footballers
Argentine expatriate men's footballers
Men's association football forwards
Club Atlético River Plate footballers
Brescia Calcio players
Ascoli Calcio 1898 FC players
UC Sampdoria players
SSD Varese Calcio players
Parma Calcio 1913 players
Feralpisalò players
Serie A players
Serie B players
Serie C players
Expatriate men's footballers in Italy |
https://en.wikipedia.org/wiki/NSP1%20%28rotavirus%29 | NSP1 (NS53), the product of rotavirus gene 5, is a nonstructural RNA-binding protein that contains a cysteine-rich region and is a component of early replication intermediates. RNA-folding predictions suggest that this region of the NSP1 mRNA can interact with itself, producing a stem-loop structure similar to that found near the 5'-terminus of the NSP1 mRNA.
The carboxyl-half of the rotavirus nonstructural protein NSP1 is not required for virus replication.
NSP1 could play a role in host range restriction.
The cysteine-rich region of NSP1 is not considered essential for genome segment reassortment with heterologous virus.
NSP1 interacts with IRF3 in the infected cell. NSP1 is an antagonist of the IFN-signaling pathway.
Interferon regulatory factor 3 (IRF3) is a key transcription factor involved in the induction of interferon (IFN) in response to viral infection. NSP1 binds to and targets IRF3 for proteasome degradation early post-infection. IRF3 degradation is dependent on the presence of NSP1 and the integrity of the N-terminal zinc-binding domain, coupled with the regulated stability of IRF3 and NSP1 by the proteasome, collectively support the hypothesis that NSP1 is an E3 ubiquitin ligase.
NSP1 could mediates the degradation of IRF3, IRF5, and IRF7 by recognizing a common element of IRF proteins, thereby allowing NSP1 to act as a broad-spectrum antagonist of IRF function.
NSP1 also inhibits activation of NFkappaB
NSP1 inhibits cellular apoptosis by directly intera |
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