The Enzyme Database

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EC 2.1.1.23      
Deleted entry:  protein-arginine N-methyltransferase. Now listed as EC 2.1.1.124 [cytochrome c]-arginine N-methyltransferase, EC 2.1.1.125 histone-arginine N-methyltransferase and EC 2.1.1.126 [myelin basic protein]-arginine N-methyltransferase
[EC 2.1.1.23 created 1972, modified 1976, modified 1983, deleted 1999]
 
 
EC 2.1.1.230     
Accepted name: 23S rRNA (adenosine1067-2′-O)-methyltransferase
Reaction: S-adenosyl-L-methionine + adenosine1067 in 23S rRNA = S-adenosyl-L-homocysteine + 2′-O-methyladenosine1067 in 23S rRNA
Other name(s): 23S rRNA A1067 2′-methyltransferase; thiostrepton-resistance methylase; nosiheptide-resistance methyltransferase
Systematic name: S-adenosyl-L-methionine:23S rRNA (adenosine1067-2′-O)-methyltransferase
Comments: The methylase that is responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bechthold, A. and Floss, H.G. Overexpression of the thiostrepton-resistance gene from Streptomyces azureus in Escherichia coli and characterization of recognition sites of the 23S rRNA A1067 2′-methyltransferase in the guanosine triphosphatase center of 23S ribosomal RNA. Eur. J. Biochem. 224 (1994) 431–437. [DOI] [PMID: 7925357]
2.  Thompson, J., Schmidt, F. and Cundliffe, E. Site of action of a ribosomal RNA methylase conferring resistance to thiostrepton. J. Biol. Chem. 257 (1982) 7915–7917. [PMID: 6806287]
3.  Thompson, J. and Cundliffe, E. Purification and properties of an RNA methylase produced by Streptomyces azureus and involved in resistance to thiostrepton. J. Gen. Microbiol. 124 (1981) 291–297.
4.  Yang, H., Wang, Z., Shen, Y., Wang, P., Jia, X., Zhao, L., Zhou, P., Gong, R., Li, Z., Yang, Y., Chen, D., Murchie, A.I. and Xu, Y. Crystal structure of the nosiheptide-resistance methyltransferase of Streptomyces actuosus. Biochemistry 49 (2010) 6440–6450. [DOI] [PMID: 20550164]
[EC 2.1.1.230 created 2011]
 
 
EC 2.1.1.231     
Accepted name: flavonoid 4′-O-methyltransferase
Reaction: S-adenosyl-L-methionine + a 4′-hydroxyflavanone = S-adenosyl-L-homocysteine + a 4′-methoxyflavanone
For diagram of naringenin methyl ethers biosynthesis, click here
Glossary: naringenin = 4′,5,7-trihydroxyflavan-4-one
Other name(s): SOMT-2; 4′-hydroxyisoflavone methyltransferase
Systematic name: S-adenosyl-L-methionine:flavonoid 4′-O-methyltransferase
Comments: The enzyme catalyses the 4′-methylation of naringenin. In vitro it catalyses the 4′-methylation of apigenin, quercetin, daidzein and genistein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kim, D.H., Kim, B.G., Lee, Y., Ryu, J.Y., Lim, Y., Hur, H.G. and Ahn, J.H. Regiospecific methylation of naringenin to ponciretin by soybean O-methyltransferase expressed in Escherichia coli. J. Biotechnol. 119 (2005) 155–162. [DOI] [PMID: 15961179]
[EC 2.1.1.231 created 2011]
 
 
EC 2.1.1.232     
Accepted name: naringenin 7-O-methyltransferase
Reaction: S-adenosyl-L-methionine + (2S)-naringenin = S-adenosyl-L-homocysteine + (2S)-sakuranetin
For diagram of naringenin methyl ethers biosynthesis, click here
Glossary: (2S)-naringenin = (2S)-5,7,4′-trihydroxyflavan-4-one
(2S)-sakuranetin = (2S)-5,4′-dihydroxy-7-methoxyflavan-4-one
Other name(s): NOMT
Systematic name: S-adenosyl-L-methionine:(2S)-5,7,4′-trihydroxyflavanone 7-O-methyltransferase
Comments: The enzyme is involved in the biosynthesis of the sakuranetin, an inducible defense mechanism of the plant Oryza sativa (Asian rice) against pathogen attack.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rakwal, R., Agrawal, G.K., Yonekura, M. and Kodama, O. Naringenin 7-O-methyltransferase involved in the biosynthesis of the flavanone phytoalexin sakuranetin from rice (Oryza sativa L.). Plant Sci. 155 (2000) 213–221. [DOI] [PMID: 10814825]
[EC 2.1.1.232 created 2011]
 
 
EC 2.1.1.233     
Accepted name: [phosphatase 2A protein]-leucine-carboxy methyltransferase
Reaction: S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine = S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester
Other name(s): leucine carboxy methyltransferase-1; LCMT1
Systematic name: S-adenosyl-L-methionine:[phosphatase 2A protein]-leucine O-methyltransferase
Comments: Methylates the C-terminal leucine of phosphatase 2A. A key regulator of protein phosphatase 2A. The methyl ester is hydrolysed by EC 3.1.1.89 (protein phosphatase methylesterase-1). Occurs mainly in the cytoplasm, Golgi region and late endosomes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  De Baere, I., Derua, R., Janssens, V., Van Hoof, C., Waelkens, E., Merlevede, W. and Goris, J. Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry 38 (1999) 16539–16547. [DOI] [PMID: 10600115]
2.  Tsai, M.L., Cronin, N. and Djordjevic, S. The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A. Acta Crystallogr. D Biol. Crystallogr. 67 (2011) 14–24. [DOI] [PMID: 21206058]
[EC 2.1.1.233 created 2011]
 
 
EC 2.1.1.234     
Accepted name: dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose N,N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose = 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose
For diagram of dTDP-D-desosamine biosynthesis, click here
Glossary: α-D-desosamine = 3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose
dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose = dTDP-D-desosamine
Other name(s): DesVI
Systematic name: S-adenosyl-L-methionine:dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose 3-N,N-dimethyltransferase
Comments: The enzyme is involved in the biosynthesis of desosamine, a 3-(dimethylamino)-3,4,6-trideoxyhexose found in certain macrolide antibiotics such as erthyromycin, azithromycin, and clarithromycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chen, H., Yamase, H., Murakami, K., Chang, C.W., Zhao, L., Zhao, Z. and Liu, H.W. Expression, purification, and characterization of two N,N-dimethyltransferases, tylM1 and desVI, involved in the biosynthesis of mycaminose and desosamine. Biochemistry 41 (2002) 9165–9183. [DOI] [PMID: 12119032]
2.  Burgie, E.S. and Holden, H.M. Three-dimensional structure of DesVI from Streptomyces venezuelae: a sugar N,N-dimethyltransferase required for dTDP-desosamine biosynthesis. Biochemistry 47 (2008) 3982–3988. [DOI] [PMID: 18327916]
[EC 2.1.1.234 created 2011]
 
 
EC 2.1.1.235     
Accepted name: dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose N,N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose = 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-α-D-glucopyranose
For diagram of dTDP-D-mycaminose biosynthesis, click here
Glossary: dTDP-D-mycaminose = dTDP-3-dimethylamino-3,6-dideoxy-α-D-glucopyranose
Other name(s): TylM1
Systematic name: S-adenosyl-L-methionine:dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose 3-N,N-dimethyltransferase
Comments: The enzyme is involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin, which is produced by the bacterium Streptomyces fradiae.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chen, H., Yamase, H., Murakami, K., Chang, C.W., Zhao, L., Zhao, Z. and Liu, H.W. Expression, purification, and characterization of two N,N-dimethyltransferases, tylM1 and desVI, involved in the biosynthesis of mycaminose and desosamine. Biochemistry 41 (2002) 9165–9183. [DOI] [PMID: 12119032]
2.  Carney, A.E. and Holden, H.M. Molecular architecture of TylM1 from Streptomyces fradiae: an N,N-dimethyltransferase involved in the production of dTDP-D-mycaminose. Biochemistry 50 (2011) 780–787. [DOI] [PMID: 21142177]
[EC 2.1.1.235 created 2011]
 
 
EC 2.1.1.236     
Accepted name: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose N,N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose = 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-α-D-galactopyranose
For diagram of dTDP-Fuc3NAc, dTDP-Fuc4NAc and dTDP-Fuc3NMe2 biosynthesis, click here
Glossary: dTDP-3-dimethylamino-3,6-dideoxy-α-D-galactopyranose = dTDP-D-ravidosamine
Other name(s): RavNMT
Systematic name: S-adenosyl-L-methionine:dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose 3-N,N-dimethyltransferase
Comments: The enzyme is involved in the synthesis of dTDP-D-ravidosamine, the amino sugar moiety of the antibiotic ravidomycin V, which is produced by the bacterium Streptomyces ravidus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kharel, M.K., Lian, H. and Rohr, J. Characterization of the TDP-D-ravidosamine biosynthetic pathway: one-pot enzymatic synthesis of TDP-D-ravidosamine from thymidine-5-phosphate and glucose-1-phosphate. Org. Biomol. Chem. 9 (2011) 1799–1808. [DOI] [PMID: 21264378]
[EC 2.1.1.236 created 2011]
 
 
EC 2.1.1.237     
Accepted name: mycinamicin III 3′′-O-methyltransferase
Reaction: S-adenosyl-L-methionine + mycinamicin III = S-adenosyl-L-homocysteine + mycinamicin IV
For diagram of mycinamycin biosynthesis, click here
Glossary: mycinamicin III = [(2R,3R,4E,6E,9R,11S,12S,13S,14E)-2-ethyl-9,11,13-trimethyl-8,16-dioxo-12-{[3,4,6-trideoxy-3-(dimethylamino)-β-D-xylo-hexopyranosyl]oxy}oxacyclohexadeca-4,6,14-trien-3-yl]methyl 6-deoxy-2-O-methyl-β-D-allopyranoside
mycinamicin IV = [(2R,3R,4E,6E,9R,11S,12S,13S,14E)-2-ethyl-9,11,13-trimethyl-8,16-dioxo-12-{[3,4,6-trideoxy-3-(dimethylamino)-β-D-xylo-hexopyranosyl]oxy}oxacyclohexadeca-4,6,14-trien-3-yl]methyl 6-deoxy-2,3-di-O-methyl-β-D-allopyranoside
Other name(s): MycF
Systematic name: S-adenosyl-L-methionine:mycinamicin III 3′′-O-methyltransferase
Comments: The enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Li, S., Anzai, Y., Kinoshita, K., Kato, F. and Sherman, D.H. Functional analysis of MycE and MycF, two O-methyltransferases involved in the biosynthesis of mycinamicin macrolide antibiotics. Chembiochem. 10 (2009) 1297–1301. [DOI] [PMID: 19415708]
[EC 2.1.1.237 created 2011]
 
 
EC 2.1.1.238     
Accepted name: mycinamicin VI 2′′-O-methyltransferase
Reaction: S-adenosyl-L-methionine + mycinamicin VI = S-adenosyl-L-homocysteine + mycinamicin III
For diagram of mycinamycin biosynthesis, click here
Glossary: mycinamicin III = [(2R,3R,4E,6E,9R,11S,12S,13S,14E)-2-ethyl-9,11,13-trimethyl-8,16-dioxo-12-{[3,4,6-trideoxy-3-(dimethylamino)-β-D-xylo-hexopyranosyl]oxy}oxacyclohexadeca-4,6,14-trien-3-yl]methyl 6-deoxy-2-O-methyl-β-D-allopyranoside
mycinamicin VI = [(2R,3R,4E,6E,9R,11S,12S,13S,14E)-2-ethyl-9,11,13-trimethyl-8,16-dioxo-12-{[3,4,6-trideoxy-3-(dimethylamino)-β-D-xylo-hexopyranosyl]oxy}oxacyclohexadeca-4,6,14-trien-3-yl]methyl 6-deoxy-β-D-allopyranoside
Other name(s): MycE
Systematic name: S-adenosyl-L-methionine:mycinamicin VI 2′′-O-methyltransferase
Comments: The enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics. Requires Mg2+ for optimal activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Li, S., Anzai, Y., Kinoshita, K., Kato, F. and Sherman, D.H. Functional analysis of MycE and MycF, two O-methyltransferases involved in the biosynthesis of mycinamicin macrolide antibiotics. Chembiochem. 10 (2009) 1297–1301. [DOI] [PMID: 19415708]
[EC 2.1.1.238 created 2011]
 
 
EC 2.1.1.239     
Accepted name: L-olivosyl-oleandolide 3-O-methyltransferase
Reaction: S-adenosyl-L-methionine + L-olivosyl-oleandolide = S-adenosyl-L-homocysteine + L-oleandrosyl-oleandolide
Other name(s): OleY
Systematic name: S-adenosyl-L-methionine:L-olivosyl-oleandolide B 3-O-methyltransferase
Comments: The enzyme is involved in the biosynthesis of the macrolide antibiotic oleandomycin in Streptomyces antibioticus. It can also act on other monoglycosylated macrolactones, including L-rhamnosyl-erythronolide B and L-mycarosyl-erythronolide B.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rodriguez, L., Rodriguez, D., Olano, C., Brana, A.F., Mendez, C. and Salas, J.A. Functional analysis of OleY L-oleandrosyl 3-O-methyltransferase of the oleandomycin biosynthetic pathway in Streptomyces antibioticus. J. Bacteriol. 183 (2001) 5358–5363. [DOI] [PMID: 11514520]
[EC 2.1.1.239 created 2012]
 
 


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