The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 2.1.1.26     
Accepted name: iodophenol O-methyltransferase
Reaction: S-adenosyl-L-methionine + 2-iodophenol = S-adenosyl-L-homocysteine + 2-iodophenol methyl ether
Systematic name: S-adenosyl-L-methionine:2-iodophenol O-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-95-4
References:
1.  Tomita, K., Cha, C.-J. and Lardy, H.A. Enzymic O-methylation of iodinated phenols and thyroid hormones. J. Biol. Chem. 239 (1964) 1202–1207. [PMID: 14165927]
[EC 2.1.1.26 created 1972]
 
 
EC 2.1.1.260     
Accepted name: rRNA small subunit pseudouridine methyltransferase Nep1
Reaction: S-adenosyl-L-methionine + pseudouridine1191 in yeast 18S rRNA = S-adenosyl-L-homocysteine + N1-methylpseudouridine1191 in yeast 18S rRNA
Other name(s): Nep1; nucleolar essential protein 1
Systematic name: S-adenosyl-L-methionine:18S rRNA (pseudouridine1191-N1)-methyltransferase
Comments: This enzyme, which occurs in both prokaryotes and eukaryotes, recognizes specific pseudouridine residues (Ψ) in small subunits of ribosomal RNA based on the local RNA structure. It recognizes Ψ914 in 16S rRNA from the archaeon Methanocaldococcus jannaschii, Ψ1191 in yeast 18S rRNA, and Ψ1248 in human 18S rRNA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Taylor, A.B., Meyer, B., Leal, B.Z., Kötter, P., Schirf, V., Demeler, B., Hart, P.J., Entian, K.-D. and Wöhnert, J. The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site. Nucleic Acids Res. 36 (2008) 1542–1554. [DOI] [PMID: 18208838]
2.  Wurm, J.P., Meyer, B., Bahr, U., Held, M., Frolow, O., Kötter, P., Engels, J.W., Heckel, A., Karas, M., Entian, K.-D. and Wöhnert, J. The ribosome assembly factor Nep1 responsible for Bowen-Conradi syndrome is a pseudouridine-N1-specific methyltransferase. Nucleic Acids Res. 38 (2010) 2387–2398. [DOI] [PMID: 20047967]
3.  Meyer, B., Wurm, J.P., Kötter, P., Leisegang, M.S., Schilling, V., Buchhaupt, M., Held, M., Bahr, U., Karas, M., Heckel, A., Bohnsack, M.T., Wöhnert, J. and Entian, K.-D. The Bowen-Conradi syndrome protein Nep1 (Emg1) has a dual role in eukaryotic ribosome biogenesis, as an essential assembly factor and in the methylation of Ψ1191 in yeast 18S rRNA. Nucleic Acids Res. 39 (2011) 1526–1537. [DOI] [PMID: 20972225]
[EC 2.1.1.260 created 2012]
 
 
EC 2.1.1.261     
Accepted name: 4-dimethylallyltryptophan N-methyltransferase
Reaction: S-adenosyl-L-methionine + 4-dimethylallyl-L-tryptophan = S-adenosyl-L-homocysteine + 4-dimethylallyl-L-abrine
For diagram of ergot alkaloid biosynthesis, click here
Glossary: 4-dimethylallyl-L-tryptophan = 4-(3-methylbut-2-enyl)-L-tryptophan;
4-dimethylallyl-L-abrine = 4-(3-methylbut-2-enyl)-L-abrine
Other name(s): fgaMT (gene name); easF (gene name)
Systematic name: S-adenosyl-L-methionine:4-(3-methylbut-2-enyl)-L-tryptophan N-methyltransferase
Comments: The enzyme catalyses a step in the pathway leading to biosynthesis of ergot alkaloids in certain fungi.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rigbers, O. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus. Overproduction and biochemical characterization of a 4-dimethylallyltryptophan N-methyltransferase. J. Biol. Chem. 283 (2008) 26859–26868. [DOI] [PMID: 18678866]
[EC 2.1.1.261 created 2012]
 
 
EC 2.1.1.262     
Accepted name: squalene methyltransferase
Reaction: 2 S-adenosyl-L-methionine + squalene = 2 S-adenosyl-L-homocysteine + 3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene (overall reaction)
(1a) S-adenosyl-L-methionine + squalene = S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrosqualene
(1b) S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrosqualene = S-adenosyl-L-homocysteine + 3,22-dimethyl-1,2,23,24-tetradehydro-2,3,22,23-tetrahydrosqualene
For diagram of botryococcus braunii BOT22 squalene and botrycoccene biosynthesis, click here
Other name(s): TMT-1; TMT-2
Systematic name: S-adenosyl-L-methionine:squalene C-methyltransferase
Comments: Two isoforms differing in their specificity were isolated from the green alga Botryococcus braunii BOT22. TMT-1 gave more of the dimethylated form whereas TMT2 gave more of the monomethylated form.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Niehaus, T.D., Kinison, S., Okada, S., Yeo, Y.S., Bell, S.A., Cui, P., Devarenne, T.P. and Chappell, J. Functional identification of triterpene methyltransferases from Botryococcus braunii race B. J. Biol. Chem. 287 (2012) 8163–8173. [DOI] [PMID: 22241476]
[EC 2.1.1.262 created 2012]
 
 
EC 2.1.1.263     
Accepted name: botryococcene C-methyltransferase
Reaction: 2 S-adenosyl-L-methionine + C30 botryococcene = 2 S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene (overall reaction)
(1a) S-adenosyl-L-methionine + C30 botryococcene = S-adenosyl-L-homocysteine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene
(1b) S-adenosyl-L-methionine + 3-methyl-1,2-didehydro-2,3-dihydrobotryococcene = S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
(2a) S-adenosyl-L-methionine + C30 botryococcene = S-adenosyl-L-homocysteine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene
(2b) S-adenosyl-L-methionine + 20-methyl-21,22-didehydro-20,21-dihydrobotryococcene = S-adenosyl-L-homocysteine + 3,20-dimethyl-1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene
For diagram of botryococcus braunii BOT22 squalene and botrycoccene biosynthesis, click here
Glossary: C30 botryococcene = (10S,13R)-10-ethenyl-2,6,10,13,17,21-hexamethyldocosa-2,5,11,16,20-pentaene
3-methyl-1,2-didehydro-2,3-dihydrobotryococcene = showacene
20-methyl-21,22-didehydro-20,21-dihydrobotryococcene = isoshowacene
Other name(s): TMT-3
Systematic name: S-adenosyl-L-methionine:botryococcene C-methyltransferase
Comments: Isolated from the green alga Botryococcus braunii BOT22. Shows a very weak activity with squalene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Niehaus, T.D., Kinison, S., Okada, S., Yeo, Y.S., Bell, S.A., Cui, P., Devarenne, T.P. and Chappell, J. Functional identification of triterpene methyltransferases from Botryococcus braunii race B. J. Biol. Chem. 287 (2012) 8163–8173. [DOI] [PMID: 22241476]
[EC 2.1.1.263 created 2012]
 
 
EC 2.1.1.264     
Accepted name: 23S rRNA (guanine2069-N7)-methyltransferase
Reaction: S-adenosyl-L-methionine + guanine2069 in 23S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
Other name(s): rlmK (gene name); 23S rRNA m7G2069 methyltransferase
Systematic name: S-adenosyl-L-methionine:23S rRNA (guanine2069-N7)-methyltransferase
Comments: The enzyme specifically methylates guanine2069 at position N7 in 23S rRNA. In γ-proteobacteria the enzyme also catalyses EC 2.1.1.173, 23S rRNA (guanine2445-N2)-methyltransferase, while in β-proteobacteria the activities are carried out by separate proteins [1]. The enzyme from the γ-proteobacterium Escherichia coli has RNA unwinding activity as well [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kimura, S., Ikeuchi, Y., Kitahara, K., Sakaguchi, Y., Suzuki, T. and Suzuki, T. Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity. Nucleic Acids Res. 40 (2012) 4071–4085. [DOI] [PMID: 22210896]
[EC 2.1.1.264 created 2012]
 
 
EC 2.1.1.265     
Accepted name: tellurite methyltransferase
Reaction: S-adenosyl-L-methionine + tellurite = S-adenosyl-L-homocysteine + methanetelluronate
Other name(s): TehB
Systematic name: S-adenosyl-L-methionine:tellurite methyltransferase
Comments: The enzyme is involved in the detoxification of tellurite. It can also methylate selenite and selenium dioxide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, M., Turner, R.J., Winstone, T.L., Saetre, A., Dyllick-Brenzinger, M., Jickling, G., Tari, L.W., Weiner, J.H. and Taylor, D.E. Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance. J. Bacteriol. 182 (2000) 6509–6513. [DOI] [PMID: 11053398]
2.  Choudhury, H.G., Cameron, A.D., Iwata, S. and Beis, K. Structure and mechanism of the chalcogen-detoxifying protein TehB from Escherichia coli. Biochem. J. 435 (2011) 85–91. [DOI] [PMID: 21244361]
[EC 2.1.1.265 created 2012]
 
 
EC 2.1.1.266     
Accepted name: 23S rRNA (adenine2030-N6)-methyltransferase
Reaction: S-adenosyl-L-methionine + adenine2030 in 23S rRNA = S-adenosyl-L-homocysteine + N6-methyladenine2030 in 23S rRNA
Other name(s): YhiR protein; rlmJ (gene name); m6A2030 methyltransferase
Systematic name: S-adenosyl-L-methionine:23S rRNA (adenine2030-N6)-methyltransferase
Comments: The recombinant RlmJ protein is most active in methylating deproteinized 23S ribosomal subunit, and does not methylate the completely assembled 50S subunits [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Golovina, A.Y., Dzama, M.M., Osterman, I.A., Sergiev, P.V., Serebryakova, M.V., Bogdanov, A.A. and Dontsova, O.A. The last rRNA methyltransferase of E. coli revealed: the yhiR gene encodes adenine-N6 methyltransferase specific for modification of A2030 of 23S ribosomal RNA. RNA 18 (2012) 1725–1734. [DOI] [PMID: 22847818]
[EC 2.1.1.266 created 2013]
 
 
EC 2.1.1.267     
Accepted name: flavonoid 3′,5′-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + a 3′-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 3′-methoxyflavonoid
(2) S-adenosyl-L-methionine + a 5′-hydroxy-3′-methoxyflavonoid = S-adenosyl-L-homocysteine + a 3′,5′-dimethoxyflavonoid
For diagram of anthocyanidin glucoside biosynthesis, click here
Glossary: delphinidin = 3,3′,4′,5,5′,7-hexahydroxyflavylium
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
myricetin = 3,3′,4′,5,5′,7-hexahydroxyflavone
quercetin = 3,3′,4′,5,7-pentahydroxyflavone
Other name(s): AOMT; CrOMT2
Systematic name: S-adenosyl-L-methionine:flavonoid 3′-O-methyltransferase
Comments: Isolated from Vitis vinifera (grape) [2]. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. The enzyme from Catharanthus roseus was most active with myricetin [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Cacace, S., Schröder, G., Wehinger, E., Strack, D., Schmidt, J. and Schröder, J. A flavonol O-methyltransferase from Catharanthus roseus performing two sequential methylations. Phytochemistry 62 (2003) 127–137. [DOI] [PMID: 12482447]
2.  Hugueney, P., Provenzano, S., Verries, C., Ferrandino, A., Meudec, E., Batelli, G., Merdinoglu, D., Cheynier, V., Schubert, A. and Ageorges, A. A novel cation-dependent O-methyltransferase involved in anthocyanin methylation in grapevine. Plant Physiol. 150 (2009) 2057–2070. [DOI] [PMID: 19525322]
[EC 2.1.1.267 created 2013, modified 2014]
 
 
EC 2.1.1.268     
Accepted name: tRNAThr (cytosine32-N3)-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + cytosine32 in tRNAThr = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
(2) S-adenosyl-L-methionine + cytosine32 in tRNASer = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Other name(s): ABP140; Trm140p
Systematic name: S-adenosyl-L-methionine:tRNAThr (cytosine32-N3)-methyltransferase
Comments: The enzyme from Saccharomyces cerevisiae specifically methylates cytosine32 in tRNAThr and in tRNASer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Noma, A., Yi, S., Katoh, T., Takai, Y., Suzuki, T. and Suzuki, T. Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae. RNA 17 (2011) 1111–1119. [DOI] [PMID: 21518805]
2.  D'Silva, S., Haider, S.J. and Phizicky, E.M. A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop. RNA 17 (2011) 1100–1110. [DOI] [PMID: 21518804]
[EC 2.1.1.268 created 2013]
 
 
EC 2.1.1.269     
Accepted name: dimethylsulfoniopropionate demethylase
Reaction: S,S-dimethyl-β-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
For diagram of 3-(dimethylsulfonio)propanoate metabolism, click here
Glossary: S,S-dimethyl-β-propiothetin = 3-(S,S-dimethylsulfonio)propanoate
Other name(s): dmdA (gene name); dimethylsulfoniopropionate-dependent demethylase A
Systematic name: S,S-dimethyl-β-propiothetin:tetrahydrofolate S-methyltransferase
Comments: The enzyme from the marine bacteria Pelagibacter ubique and Ruegeria pomeroyi are specific towards S,S-dimethyl-β-propiothetin. They do not demethylate glycine-betaine [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jansen, M. and Hansen, T.A. Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria. Arch. Microbiol. 169 (1998) 84–87. [PMID: 9396840]
2.  Reisch, C.R., Moran, M.A. and Whitman, W.B. Dimethylsulfoniopropionate-dependent demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi. J. Bacteriol. 190 (2008) 8018–8024. [DOI] [PMID: 18849431]
3.  Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B. and Lanzilotta, W.N. Structures of dimethylsulfoniopropionate-dependent demethylase from the marine organism Pelagibacter ubique. Protein Sci. 21 (2012) 289–298. [DOI] [PMID: 22162093]
[EC 2.1.1.269 created 2013]
 
 


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