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https://en.wikipedia.org/wiki/5-Methyltetrahydropteroyltriglutamate%E2%80%94homocysteine%20S-methyltransferase | In enzymology, a 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine tetrahydropteroyltri-L-glutamate + L-methionine
Thus, the two substrates of this enzyme are 5-methyltetrahydropteroyltri-L-glutamate and L-homocysteine, whereas its two products are tetrahydropteroyltri-L-glutamate and L-methionine. This enzyme participates in methionine metabolism. It has 2 cofactors: orthophosphate, and zinc.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5-methyltetrahydropteroyltri-L-glutamate:L-homocysteine S-methyltransferase. Other names in common use include tetrahydropteroyltriglutamate methyltransferase, homocysteine methylase, methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase, methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase, cobalamin-independent methionine synthase, methionine synthase (cobalamin-independent), and MetE.
Structure
The enzyme from Escherichia coli consists of two alpha8-beta8 (TIM) barrels positioned face to face and thought to have evolved by gene duplication. The active site lies between the tops of the two barrels, the N-terminal barrel binds 5-methyltetrahydropteroyltri-L-glutamic acid and the C-terminal barrel binds homocysteine. Homocysteine is co |
https://en.wikipedia.org/wiki/6-hydroxymellein%20O-methyltransferase | In enzymology, a 6-hydroxymellein O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 6-hydroxymellein S-adenosyl-L-homocysteine + 6-methoxymellein
Thus, the two substrates of this enzyme are S-adenosyl methionine and 6-hydroxymellein, whereas its two products are S-adenosylhomocysteine and 6-methoxymellein.
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:6-hydroxymellein 6-O-methyltransferase. This enzyme is also called 6-hydroxymellein methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-O-methylnorlaudanosoline%205%27-O-methyltransferase | In enzymology, a 6-O-methylnorlaudanosoline 5'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 6-O-methylnorlaudanosoline S-adenosyl-L-homocysteine + nororientaline
Thus, the two substrates of this enzyme are S-adenosyl methionine and 6-O-methylnorlaudanosoline, whereas its two products are S-adenosylhomocysteine and nororientaline.
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:6-O-methylnorlaudanosoline 5'-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/7-methylxanthosine%20synthase | In enzymology, a 7-methylxanthosine synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + xanthosine S-adenosyl-L-homocysteine + 7-methylxanthosine
Thus, the two substrates of this enzyme are S-adenosyl methionine and xanthosine, whereas its two products are S-adenosylhomocysteine and 7-methylxanthosine.
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:xanthosine N7-methyltransferase. Other names in common use include xanthosine methyltransferase, XMT, xanthosine:S-adenosyl-L-methionine methyltransferase, CtCS1, CmXRS1, CaXMT1, and S-adenosyl-L-methionine:xanthosine 7-N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/8-hydroxyquercetin%208-O-methyltransferase | In enzymology, a 8-hydroxyquercetin 8-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3,5,7,8,3',4'-hexahydroxyflavone S-adenosyl-L-homocysteine + 3,5,7,3',4'-pentahydroxy-8-methoxyflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3,5,7,8,3',4'-hexahydroxyflavone (gossypetin), whereas its two products are S-adenosylhomocysteine and 3,5,7,3',4'-pentahydroxy-8-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:3,5,7,8,3',4'-hexahydroxyflavone 8-O-methyltransferase. Other names in common use include flavonol 8-O-methyltransferase, flavonol 8-methyltransferase, S-adenosyl-L-methionine:3,3',4',5,7,8-hexahydroxyflavone, 8-O-methyltransferase, and 8-hydroxyquercitin 8-O-methyltransferase [mis-spelt].
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Amine%20N-methyltransferase | Amine N-methyltransferase (), also called indolethylamine N-methyltransferase, and thioether S-methyltransferase, is an enzyme that is ubiquitously present in non-neural tissues and catalyzes the N-methylation of tryptamine and structurally related compounds. More recently, it was discovered that this enzyme can also catalyze the methylation of thioether and selenoether compounds, although the physiological significance of this biotransformation is not yet known.
The chemical reaction taking place is:
S-adenosyl-L-methionine + an amine S-adenosyl-L-homocysteine + a methylated amine
Thus, the two substrates of this enzyme are S-adenosyl methionine and amine, whereas its two products are S-adenosylhomocysteine and methylated amine. In the case of tryptamine and serotonin these then become the dimethylated indolethylamines N,N-dimethyltryptamine (DMT) and bufotenine respectively.
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:amine N-methyltransferase. Other names in common use include nicotine N-methyltransferase, tryptamine N-methyltransferase, indolethylamine N-methyltransferase, and arylamine N-methyltransferase. This enzyme participates in tryptophan metabolism.
A wide range of primary, secondary and tertiary amines can act as acceptors, including tryptamine, aniline, nicotine and a variety of drugs and other xenobiotics.
Struct |
https://en.wikipedia.org/wiki/Anthranilate%20N-methyltransferase | In enzymology, an anthranilate N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + anthranilate S-adenosyl-L-homocysteine + N-methylanthranilate
Thus, the two substrates of this enzyme are S-adenosyl methionine and anthranilate, whereas its two products are S-adenosylhomocysteine and N-methylanthranilate.
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:anthranilate N-methyltransferase. This enzyme is also called anthranilic acid N-methyltransferase. This enzyme participates in acridone alkaloid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure
Anthranilates |
https://en.wikipedia.org/wiki/Apigenin%204%27-O-methyltransferase | In enzymology, an apigenin 4'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 5,7,4'-trihydroxyflavone S-adenosyl-L-homocysteine + 4'-methoxy-5,7-dihydroxyflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5,7,4'-trihydroxyflavone (apigenin), whereas its two products are S-adenosylhomocysteine and 4'-methoxy-5,7-dihydroxyflavone (acacetin).
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:5,7,4'-trihydroxyflavone 4'-O-methyltransferase. Other names in common use include flavonoid O-methyltransferase, and flavonoid 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/Betaine%E2%80%94homocysteine%20S-methyltransferase | In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively:
Trimethylglycine (methyl donor) + homocysteine (hydrogen donor) → dimethylglycine (hydrogen receiver) + methionine (methyl receiver)
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. This enzyme participates in the metabolism of glycine, serine, threonine and also methionine.
Isozymes
In humans, there are two isozymes, BHMT and BHMT2, each encoded by a separate gene.
Tissue distribution
BHMT is expressed most predominantly in the liver and kidney.
Clinical significance
Mutations in the BHMT gene are known to exist in humans. Anomalies may influence the metabolism of homocysteine , which is implicated in disorders ranging from vascular disease, autism, and schizophrenia to neural tube birth defects such as spina bifida.
See also
Betaine
References
Further reading
External links
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Caffeate%20O-methyltransferase | In enzymology, a caffeate O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3,4-dihydroxy-trans-cinnamate (caffeic acid), whereas its two products are S-adenosylhomocysteine and 3-methoxy-4-hydroxy-trans-cinnamate (ferulic 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:3,4-dihydroxy-trans-cinnamate 3-O-methyltransferase. Other names in common use include caffeate methyltransferase, caffeate 3-O-methyltransferase, and ''S-adenosyl-L-methionine:caffeic acid-O''-methyltransferase. This enzyme participates in phenylpropanoid 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
O-methylated hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/Caffeoyl-CoA%20O-methyltransferase | In enzymology, a caffeoyl-CoA O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + caffeoyl-CoA S-adenosyl-L-homocysteine + feruloyl-CoA
Thus, the two substrates of this enzyme are S-adenosyl methionine and caffeoyl-CoA, whereas its two products are S-adenosylhomocysteine and feruloyl-CoA. A large number of natural products are generated via a step involving this enzyme.
This enzyme is classified to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:caffeoyl-CoA 3-O-methyltransferase. Other names in common use include caffeoyl coenzyme A methyltransferase, caffeoyl-CoA 3-O-methyltransferase, and trans-caffeoyl-CoA 3-O-methyltransferase. This enzyme participates in phenylpropanoid 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
O-methylated hydroxycinnamic acids metabolism
O-methylation |
https://en.wikipedia.org/wiki/Calmodulin-lysine%20N-methyltransferase | In enzymology, a calmodulin-lysine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + calmodulin L-lysine S-adenosyl-L-homocysteine + calmodulin N6-methyl-L-lysine
Thus, the two substrates of this enzyme are S-adenosyl methionine and calmodulin L-lysine, whereas its two products are S-adenosylhomocysteine and calmodulin N6-methyl-L-lysine.
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:calmodulin-L-lysine N6-methyltransferase. Other names in common use include S-adenosylmethionine:calmodulin (lysine) N-methyltransferase, and S-adenosyl-L-methionine:calmodulin-L-lysine 6-N-methyltransferase. This enzyme participates in lysine degradation.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carnosine%20N-methyltransferase | In enzymology, a carnosine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + carnosine S-adenosyl-L-homocysteine + anserine
Thus, the two substrates of this enzyme are S-adenosyl methionine and carnosine, whereas its two products are S-adenosylhomocysteine and anserine.
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:carnosine N-methyltransferase. This enzyme participates in histidine metabolism.
Gene
The genes encoding carnosine N-methyltransferase activity have been identified by Jakub Drozak and coworkers in 2013 and 2015. In birds and reptiles, the enzyme is encoded by histamine N-methyltransferase-like gene (HNMT-like). Importantly, the HNMT-like gene is absent from available mammalian genomes and in mammalian species, the formation of anserine is catalyzed by methyltransferase that is unrelated to the reptilian and avian enzyme and encoded by C9orf41/UPF0586 gene.
Protein Nomenclature
Currently, the avian-reptilian enzyme encoded by HNMT-like gene is labeled as carnosine N-methyltransferase 2 in public databases, while the mammalian methyltransferase is named carnosine N-methyltransferase 1 (CARNMT1).
References
Further reading
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chlorophenol%20O-methyltransferase | In enzymology, a chlorophenol O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + trichlorophenol S-adenosyl-L-homocysteine + trichloroanisole
Thus, the two substrates of this enzyme are S-adenosyl methionine and trichlorophenol, whereas its two products are S-adenosylhomocysteine and trichloroanisole.
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:trichlorophenol O-methyltransferase. Other names in common use include halogenated phenol O-methyltransferase, trichlorophenol, and O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cobalt-factor%20II%20C20-methyltransferase | In enzymology, a cobalt-factor II C20-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + cobalt-factor II S-adenosyl-L-homocysteine + cobalt-factor III
The two substrates of this enzyme are S-adenosyl methionine and cobalt-factor II; its two products are S-adenosylhomocysteine and cobalt-factor III.
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:cobalt-factor-II C20-methyltransferase. This enzyme is also called CbiL. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria such as Salmonella typhimurium and Bacillus megaterium.
See also
Cobalamin biosynthesis
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Columbamine%20O-methyltransferase | In enzymology, a columbamine O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + columbamine S-adenosyl-L-homocysteine + palmatine
Thus, the two substrates of this enzyme are S-adenosyl methionine and columbamine, whereas its two products are S-adenosylhomocysteine and palmatine.
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:columbamine O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Corydaline%20synthase | In enzymology, a corydaline synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + palmatine + 2 NADPH + H+ S-adenosyl-L-homocysteine + corydaline + 2 NADP+
The 4 substrates of this enzyme are S-adenosyl methionine, palmatine, NADPH, and H+, whereas its 3 products are S-adenosylhomocysteine, corydaline, and NADP+.
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:protoberberine 13-C-methyltransferase.
References
EC 2.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cycloartenol%2024-C-methyltransferase | In enzymology, a cycloartenol 24-C-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + cycloartenol S-adenosyl-L-homocysteine + (24R)-24-methylcycloart-25-en-3beta-ol
Thus, the two substrates of this enzyme are S-adenosyl methionine and cycloartenol, whereas its two products are S-adenosylhomocysteine and (24R)-24-methylcycloart-25-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:cycloartenol 24-C-methyltransferase. This enzyme is also called sterol C-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclopropane-fatty-acyl-phospholipid%20synthase | In enzymology, a cyclopropane-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 cyclopropane 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 cyclopropane 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 (cyclizing). Other names in common use include cyclopropane synthetase, unsaturated-phospholipid methyltransferase, cyclopropane synthase, cyclopropane fatty acid synthase, cyclopropane fatty acid synthetase, and CFA synthase.
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/%28cytochrome%20c%29-arginine%20N-methyltransferase | In enzymology, a [cytochrome c]-arginine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + [cytochrome c]-arginine S-adenosyl-L-homocysteine + [cytochrome c]-Nomega-methyl-arginine
Thus, the two substrates of this enzyme are S-adenosyl methionine and cytochrome c-arginine, whereas its two products are S-adenosylhomocysteine and cytochrome c-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:[cytochrome c]-arginine Nomega-methyltransferase. Other names in common use include S-adenosyl-L-methionine:[cytochrome c]-arginine, and omega-N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28cytochrome%20c%29-lysine%20N-methyltransferase | In enzymology, a [cytochrome c]-lysine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + [cytochrome c]-L-lysine S-adenosyl-L-homocysteine + [cytochrome c]-N-methyl-L-lysine
Thus, the two substrates of this enzyme are S-adenosyl methionine and cytochrome c-L-lysine, whereas its two products are S-adenosylhomocysteine and cytochrome c-N6-methyl-L-lysine.
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:[cytochrome c]-L-lysine N6-methyltransferase. Other names in common use include cytochrome c (lysine) methyltransferase, cytochrome c methyltransferase, cytochrome c-specific protein methylase III, cytochrome c-specific protein-lysine methyltransferase, S-adenosyl-L-methionine:[cytochrome c]-L-lysine, and 6-N-methyltransferase. This enzyme participates in lysine degradation.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28cytochrome%20c%29-methionine%20S-methyltransferase | In enzymology, a [cytochrome-c]-methionine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + [cytochrome c]-methionine S-adenosyl-L-homocysteine + [cytochrome c]-S-methyl-methionine
Thus, the two substrates of this enzyme are S-adenosyl methionine and cytochrome c methionine, whereas its two products are S-adenosylhomocysteine and cytochrome c-S-methyl-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:[cytochrome c]-methionine S-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Demethylmacrocin%20O-methyltransferase | In enzymology, a demethylmacrocin O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + demethylmacrocin S-adenosyl-L-homocysteine + macrocin
Thus, the two substrates of this enzyme are S-adenosyl methionine and demethylmacrocin, whereas its two products are S-adenosylhomocysteine and macrocin.
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:demethylmacrocin 2"'-O-methyltransferase. This enzyme is also called demethylmacrocin methyltransferase. This enzyme participates in biosynthesis of 12-, 14- and 16-membered macrolides.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Demethylsterigmatocystin%206-O-methyltransferase | In enzymology, a demethylsterigmatocystin 6-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 6-demethylsterigmatocystin S-adenosyl-L-homocysteine + sterigmatocystin
Thus, the two substrates of this enzyme are S-adenosyl methionine and 6-demethylsterigmatocystin, whereas its two products are S-adenosylhomocysteine and sterigmatocystin.
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:6-demethylsterigmatocystin 6-O-methyltransferase. Other names in common use include demethylsterigmatocystin methyltransferase, and O-methyltransferase I.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deoxycytidylate%20C-methyltransferase | In enzymology, a deoxycytidylate C-methyltransferase () is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydrofolate + dCMP dihydrofolate + deoxy-5-methylcytidylate
Thus, the two substrates of this enzyme are 5,10-Methylenetetrahydrofolic acid and dCMP, whereas its two products are dihydrofolic acid and deoxy-5-methylcytidylic acid.
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:dCMP C-methyltransferase. Other names in common use include deoxycytidylate methyltransferase, and dCMP methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dimethylhistidine%20N-methyltransferase | In enzymology, a dimethylhistidine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + Nalpha,Nalpha-dimethyl-L-histidine S-adenosyl-L-homocysteine + Nalpha,Nalpha,Nalpha-trimethyl-L-histidine
Thus, the two substrates of this enzyme are S-adenosyl methionine and Nalpha,Nalpha-dimethyl-L-histidine, whereas its two products are S-adenosylhomocysteine and Nalpha,Nalpha,Nalpha-trimethyl-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:Nalpha,Nalpha-dimethyl-L-histidine Nalpha-methyltransferase. Other names in common use include dimethylhistidine methyltransferase, histidine-alpha-N-methyltransferase, S-adenosyl-L-methionine:alpha-N,alpha-N-dimethyl-L-histidine, and alpha-N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diphthine%20synthase | In enzymology, a diphthine synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine S-adenosyl-L-homocysteine + 2-[3-carboxy-3-(methylammonio)propyl]-L-histidine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 2-(3-carboxy-3-aminopropyl)-L-histidine, whereas its two products are S-adenosylhomocysteine and [[2-[3-carboxy-3-(methylammonio)propyl]-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:2-(3-carboxy-3-aminopropyl)-L-histidine methyltransferase. Other names in common use include S-adenosyl-L-methionine:elongation factor 2 methyltransferase, and diphthine methyltransferase.
Structural studies
As of late 2007, 84 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/Fatty-acid%20O-methyltransferase | In enzymology, a fatty-acid O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + a fatty acid S-adenosyl-L-homocysteine + a fatty acid methyl ester
Thus, the two substrates of this enzyme are S-adenosyl methionine and fatty acid, whereas its two products are S-adenosylhomocysteine and fatty acid 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:fatty-acid O-methyltransferase. Other names in common use include fatty acid methyltransferase, and fatty acid O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucuronoxylan%204-O-methyltransferase | In enzymology, a glucuronoxylan 4-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + glucuronoxylan D-glucuronate S-adenosyl-L-homocysteine + glucuronoxylan 4-O-methyl-D-glucuronate
Thus, the two substrates of this enzyme are S-adenosyl methionine and glucuronoxylan D-glucuronate, whereas its two products are S-adenosylhomocysteine and glucuronoxylan 4-O-methyl-D-glucuronate.
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:glucuronoxylan-D-glucuronate 4-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%20N-methyltransferase | In enzymology, a glycine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + glycine S-adenosyl-L-homocysteine + sarcosine
Thus, the substrates of this enzyme are S-adenosyl methionine and glycine, whereas its two products are S-adenosylhomocysteine and sarcosine.
Glycine N-methyltransferase belongs to the family of methyltransferase enzymes. The systematic name of this enzyme class is S-adenosyl-L-methionine:glycine N-methyltransferase. Other names in common use include glycine methyltransferase, S-adenosyl-L-methionine:glycine methyltransferase, and GNMT. This family of enzymes participates in the metabolism of multiple amino acids.
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Viral%20nonstructural%20protein | In virology, a nonstructural protein is a protein encoded by a virus but that is not part of the viral particle. They typically include the various enzymes and transcription factors the virus uses to replicate itself, such as a viral protease (3CL/nsp5, etc.), an RNA replicase or other template-directed polymerases, and some means to control the host.
Examples
NSP1 (rotavirus)
NSP4 (rotavirus)
NSP5 (rotavirus)
Influenza non-structural protein
NS1 influenza protein
HBcAg, core antigen of hepatitis B
Bunyaviridae nonstructural S proteins
See also
Viral structural protein
References |
https://en.wikipedia.org/wiki/Guanidinoacetate%20N-methyltransferase | Guanidinoacetate N-methyltransferase () is an enzyme that catalyzes the chemical reaction and is encoded by gene GAMT located on chromosome 19p13.3.
S-adenosyl-L-methionine + guanidinoacetate S-adenosyl-L-homocysteine + creatine
Thus, the two substrates of this enzyme are S-adenosyl methionine and guanidinoacetate, whereas its two products are S-adenosylhomocysteine and creatine.
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-guanidinoacetate methyltransferase. Other names in common use include GA methylpherase, guanidinoacetate methyltransferase, guanidinoacetate transmethylase, methionine-guanidinoacetic transmethylase, and guanidoacetate methyltransferase. This enzyme participates in glycine, serine and threonine metabolism and arginine and proline metabolism.
The protein encoded by this gene is a methyltransferase that converts guanidoacetate to creatine, using S-adenosylmethionine as the methyl donor. Defects in this gene have been implicated in neurologic syndromes and muscular hypotonia, probably due to creatine deficiency and accumulation of guanidinoacetate in the brain of affected individuals. Two transcript variants encoding different isoforms have been described for this gene.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
See |
https://en.wikipedia.org/wiki/Hexaprenyldihydroxybenzoate%20methyltransferase | In enzymology, a hexaprenyldihydroxybenzoate methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 3-hexaprenyl-4,5-dihydroxybenzoate S-adenosyl-L-homocysteine + 3-hexaprenyl-4-hydroxy-5-methoxybenzoate
Thus, the two substrates of this enzyme are S-adenosyl methionine and 3-hexaprenyl-4,5-dihydroxybenzoate, whereas its two products are S-adenosylhomocysteine and 3-hexaprenyl-4-hydroxy-5-methoxybenzoate.
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-hexaprenyl-4,5-dihydroxylate O-methyltransferase. Other names in common use include 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase, and dihydroxyhexaprenylbenzoate methyltransferase. This enzyme participates in ubiquinone biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Homocysteine%20S-methyltransferase | In enzymology, a homocysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-methylmethionine + L-homocysteine 2 L-methionine
Thus, the two substrates of this enzyme are S-methylmethionine and L-homocysteine, and it produces 2 molecules of 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-homocysteine S-methyltransferase. This enzyme participates in methionine metabolism.
Alternative names
Other names of this enzyme in common use include S-adenosylmethionine homocysteine transmethylase, S-methylmethionine homocysteine transmethylase, adenosylmethionine transmethylase, methylmethionine:homocysteine methyltransferase, adenosylmethionine:homocysteine methyltransferase, homocysteine methylase, homocysteine methyltransferase, homocysteine transmethylase, L-homocysteine S-methyltransferase, S-adenosyl-L-methionine:L-homocysteine methyltransferase, S-adenosylmethionine-homocysteine transmethylase, and S-adenosylmethionine:homocysteine methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Indolepyruvate%20C-methyltransferase | In enzymology, an indolepyruvate C-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + (indol-3-yl)pyruvate S-adenosyl-L-homocysteine + (3S)-3-(indol-3-yl)-3-oxobutanoate
Thus, the two substrates of this enzyme are S-adenosyl methionine and (indol-3-yl)pyruvate, whereas its two products are S-adenosylhomocysteine and (3S)-3-(indol-3-yl)-3-oxobutanoate.
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: (indol-3-yl)pyruvate C-methyltransferase. Other names in common use include indolepyruvate methyltransferase, indolepyruvate 3-methyltransferase, indolepyruvic acid methyltransferase, and S-adenosyl-L-methionine:indolepyruvate C-methyltransferase. This enzyme participates in tryptophan metabolism.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inositol%201-methyltransferase | In enzymology, an inositol 1-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + myo-inositol S-adenosyl-L-homocysteine + 1D-1-O-methyl-myo-inositol
Thus, the two substrates of this enzyme are S-adenosyl methionine and myo-inositol, whereas its two products are S-adenosylhomocysteine and 1D-1-O-methyl-myo-inositol.
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:1D-myo-inositol 1-O-methyltransferase. Other names in common use include inositol D-1-methyltransferase, S-adenosylmethionine:myo-inositol 3-methyltransferase, myo-inositol 3-O-methyltransferase, inositol 3-O-methyltransferase (name based on 1L-numbering system, and not 1D-numbering), and S-adenosyl-L-methionine:myo-inositol 3-O-methyltransferase. This enzyme participates in inositol phosphate metabolism.
References
EC 2.1.1
Enzymes of unknown structure
Inositol |
https://en.wikipedia.org/wiki/Inositol%203-methyltransferase | In enzymology, an inositol 3-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + myo-inositol S-adenosyl-L-homocysteine + 1D-3-O-methyl-myo-inositol
Thus, the two substrates of this enzyme are S-adenosyl methionine and myo-inositol, whereas its two products are S-adenosylhomocysteine and 1D-3-O-methyl-myo-inositol.
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:1D-myo-inositol 3-O-methyltransferase. Other names in common use include inositol L-1-methyltransferase, myo-inositol 1-methyltransferase, S-adenosylmethionine:myo-inositol 1-methyltransferase, myo-inositol 1-O-methyltransferase (name based on 1L-numbering, system and not 1D-numbering), and S-adenosyl-L-methionine:myo-inositol 1-O-methyltransferase. This enzyme participates in inositol phosphate metabolism.
References
EC 2.1.1
Enzymes of unknown structure
Inositol |
https://en.wikipedia.org/wiki/Inositol%204-methyltransferase | In enzymology, an inositol 4-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + myo-inositol S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
Thus, the two substrates of this enzyme are S-adenosyl methionine and myo-inositol, whereas its two products are S-adenosylhomocysteine and 1D-4-O-methyl-myo-inositol.
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:1D-myo-inositol 4-methyltransferase. Other names in common use include myo-inositol 4-O-methyltransferase, S-adenosyl-L-methionine:myo-inositol 4-O-methyltransferase, and myo-inositol 6-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure
Inositol |
https://en.wikipedia.org/wiki/Iodophenol%20O-methyltransferase | In enzymology, an iodophenol O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 2-iodophenol S-adenosyl-L-homocysteine + 2-iodophenol methyl ether
Thus, the two substrates of this enzyme are S-adenosyl methionine and 2-iodophenol, whereas its two products are S-adenosylhomocysteine and 2-iodophenol methyl ether.
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:2-iodophenol O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isobutyraldoxime%20O-methyltransferase | In enzymology, an isobutyraldoxime O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 2-methylpropanal oxime S-adenosyl-L-homocysteine + 2-methylpropanal O-methyloxime
Thus, the two substrates of this enzyme are S-adenosyl methionine and 2-methylpropanal oxime, whereas its two products are S-adenosylhomocysteine and 2-methylpropanal O-methyloxime.
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:2-methylpropanal-oxime O-methyltransferase. Other names in common use include aldoxime methyltransferase, S-adenosylmethionine:aldoxime O-methyltransferase, and aldoxime O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28Iso%29eugenol%20O-methyltransferase | In enzymology, a (iso)eugenol O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + isoeugenol S-adenosyl-L-homocysteine + isomethyleugenol
Thus, the two substrates of this enzyme are S-adenosyl methionine and isoeugenol, whereas its two products are S-adenosylhomocysteine and isomethyleugenol.
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:isoeugenol O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isoflavone%204%27-O-methyltransferase | In enzymology, an isoflavone 4'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + an isoflavone S-adenosyl-L-homocysteine + a 4'-O-methylisoflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and isoflavone, whereas its two products are S-adenosylhomocysteine and 4'-O-methylisoflavone.
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:isoflavone 4'-O-methyltransferase. Other names in common use include 4'-hydroxyisoflavone methyltransferase, isoflavone methyltransferase, and isoflavone O-methyltransferase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure
Isoflavonoids metabolism
O-methylated flavonoids metabolism |
https://en.wikipedia.org/wiki/Isoflavone%207-O-methyltransferase | In enzymology, an isoflavone 7-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + a 7-hydroxyisoflavone S-adenosyl-L-homocysteine + a 7-methoxyisoflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 7-hydroxyisoflavone, whereas its two products are S-adenosylhomocysteine and 7-methoxyisoflavone.
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:hydroxyisoflavone 7-O-methyltransferase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure
Isoflavonoids metabolism
O-methylated flavonoids metabolism |
https://en.wikipedia.org/wiki/Isoliquiritigenin%202%27-O-methyltransferase | In enzymology, an isoliquiritigenin 2'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + isoliquiritigenin S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
Thus, the two substrates of this enzyme are S-adenosyl methionine and isoliquiritigenin, whereas its two products are S-adenosylhomocysteine and 2'-O-methylisoliquiritigenin.
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:isoliquiritigenin 2'-O-methyltransferase. Other names in common use include chalcone OMT, and CHMT.
References
EC 2.1.1
Enzymes of unknown structure
Chalconoids metabolism |
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 |
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