Enzyme Nomenclature

EC 2.1.1 (continued)

Methyltransferases

Continued from:
EC 2.1.1.1 to EC 2.1.1.50
EC 2.1.1.51 to EC 2.1.1.100
EC 2.1.1.101 to EC 2.1.1.150
EC 2.1.1.151 to EC 2.1.1.200
See separate file for EC 2.1.1.251 to EC 2.1.1.300 and EC 2.1.1.301 to EC 2.1.1.363.

Contents

EC 2.1.1.201 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase
EC 2.1.1.202 multisite-specific tRNA:(cytosine-C5)-methyltransferase
EC 2.1.1.203 tRNA (cytosine34-C5)-methyltransferase
EC 2.1.1.204 RNA (cytosine38-C5)-methyltransferase
EC 2.1.1.205 tRNA (cytidine32/guanosine34-2'-O)-methyltransferase
EC 2.1.1.206 tRNA (cytidine56-2'-O)-methyltransferase
EC 2.1.1.207 tRNA (cytidine34-2'-O)-methyltransferase
EC 2.1.1.208 23S rRNA (uridine2479-2'-O)-methyltransferase
EC 2.1.1.209 23S rRNA (guanine2535-N1)-methyltransferase
EC 2.1.1.210 demethylspheroidene O-methyltransferase
EC 2.1.1.211 tRNASer (uridine44-2'-O)-methyltransferase
EC 2.1.1.212 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase
EC 2.1.1.213 tRNA (guanine10-N2)-dimethyltransferase
EC 2.1.1.214 tRNA (guanine10-N2)-methyltransferase
EC 2.1.1.215 tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase
EC 2.1.1.216 tRNA (guanine26-N2)-dimethyltransferase
EC 2.1.1.217 tRNA (adenine22-N1)-methyltransferase
EC 2.1.1.218 tRNA (adenine9-N1)-methyltransferase
EC 2.1.1.219 tRNA (adenine57-N1/adenine58-N1)-methyltransferase
EC 2.1.1.220 tRNA (adenine58-N1)-methyltransferase
EC 2.1.1.221 tRNA (guanine9-N1)-methyltransferase
EC 2.1.1.222 2-polyprenyl-6-hydroxyphenyl methylase
EC 2.1.1.223 tRNA1Val (adenine37-N6)-methyltransferase
EC 2.1.1.224 23S rRNA (adenine2503-C8)-methyltransferase
EC 2.1.1.225 tRNA:m4X modification enzyme
EC 2.1.1.226 23S rRNA (cytidine1920-2'-O)-methyltransferase
EC 2.1.1.227 16S rRNA (cytidine1409-2'-O)-methyltransferase
EC 2.1.1.228 tRNA (guanine37-N1)-methyltransferase
EC 2.1.1.229 tRNA (carboxymethyluridine34-5-O)-methyltransferase
EC 2.1.1.230 23S rRNA (adenosine1067-2'-O)-methyltransferase
EC 2.1.1.231 flavonoid 4'-O-methyltransferase
EC 2.1.1.232 naringenin 7-O-methyltransferase
EC 2.1.1.233 [phosphatase 2A protein]-leucine-carboxy methyltransferase
EC 2.1.1.234 dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose N,N-dimethyltransferase
EC 2.1.1.235 dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose N,N-dimethyltransferase
EC 2.1.1.236 dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose N,N-dimethyltransferase
EC 2.1.1.237 mycinamicin III 3"-O-methyltransferase
EC 2.1.1.238 mycinamicin VI 2"-O-methyltransferase
EC 2.1.1.239 L-olivosyl-oleandolide 3-O-methyltransferase
EC 2.1.1.240 trans-resveratrol di-O-methyltransferase
EC 2.1.1.241 2,4,7-trihydroxy-1,4-benzoxazin-3-one-glucoside 7-O-methyltransferase
EC 2.1.1.242 16S rRNA (guanine1516-N2)-methyltransferase
EC 2.1.1.243 2-ketoarginine methyltransferase
EC 2.1.1.244 protein N-terminal methyltransferase
EC 2.1.1.245 5-methyltetrahydrosarcinapterin—corrinoid/iron-sulfur protein Co-methyltransferase
EC 2.1.1.246 [methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase
EC 2.1.1.247 [methyl-Co(III) methylamine-specific corrinoid protein]—coenzyme M methyltransferase
EC 2.1.1.248 methylamine—corrinoid protein Co-methyltransferase
EC 2.1.1.249 dimethylamine—corrinoid protein Co-methyltransferase
EC 2.1.1.250 trimethylamine—corrinoid protein Co-methyltransferase

See the following files for:
EC 2.1.1.251 to EC 2.1.1.300
EC 2.1.1.301 to EC 2.1.1.363

Entries

EC 2.1.1.201

Accepted name: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase

Reaction: S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol = S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol

For diagram of reaction click here.

Other name(s): ubiE (gene name, ambiguous)

Systematic name: S-adenosyl-L-methionine:2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol 5-C-methyltransferase

Comments: This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant [3]. The bifunctional enzyme from Escherichia coli also catalyses the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163) [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Lee, P.T., Hsu, A.Y., Ha, H.T. and Clarke, C.F. A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene. J. Bacteriol. 179 (1997) 1748-1754. [PMID: 9045837]

2. Young, I.G., McCann, L.M., Stroobant, P. and Gibson, F. Characterization and genetic analysis of mutant strains of Escherichia coli K-12 accumulating the biquinone precursors 2-octaprenyl-6-methoxy-1,4-benzoquinone and 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone. J. Bacteriol. 105 (1971) 769-778. [PMID: 4323297]

3. Dibrov, E., Robinson, K.M. and Lemire, B.D. The COQ5 gene encodes a yeast mitochondrial protein necessary for ubiquinone biosynthesis and the assembly of the respiratory chain. J. Biol. Chem. 272 (1997) 9175-9181. [PMID: 9083048]

4. Barkovich, R.J., Shtanko, A., Shepherd, J.A., Lee, P.T., Myles, D.C., Tzagoloff, A. and Clarke, C.F. Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis. J. Biol. Chem. 272 (1997) 9182-9188. [PMID: 9083049]

[EC 2.1.1.201 created 2011]

EC 2.1.1.202

Accepted name: multisite-specific tRNA:(cytosine-C5)-methyltransferase

Reaction: (1) S-adenosyl-L-methionine + cytosine34 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
(2) S-adenosyl-L-methionine + cytosine40 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA precursor
(3) S-adenosyl-L-methionine + cytosine48 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
(4) S-adenosyl-L-methionine + cytosine49 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA

Other name(s): multisite-specific tRNA:m5C-methyltransferase; TRM4 (gene name, gene corresponding to ORF YBL024w)

Systematic name: S-adenosyl-L-methionine:tRNA (cytosine-C5)-methyltransferase

Comments: The enzyme from Saccharomyces cerevisiae is responsible for complete 5-methylcytosine methylations of yeast tRNA. The incidence of modification depends on the cytosine position in tRNA. At positions 34 and 40, 5-methylcytosine is found only in two yeast tRNAs (tRNALeu(CUA) and tRNAPhe(GAA), respectively), whereas most other elongator yeast tRNAs bear either 5-methylcytosine48 or 5-methylcytosine49, but never both in the same tRNA molecule [1]. The formation of 5-methylcytosine34 and 5-methylcytosine40 is a strictly intron-dependent process, whereas the formation of 5-methylcytosine48 and 5-methylcytosine49 is an intron-independent process [2,3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Motorin, Y. and Grosjean, H. Multisite-specific tRNA:m5C-methyltransferase (Trm4) in yeast Saccharomyces cerevisiae: identification of the gene and substrate specificity of the enzyme. RNA 5 (1999) 1105-1118. [PMID: 10445884]

2. Jiang, H.Q., Motorin, Y., Jin, Y.X. and Grosjean, H. Pleiotropic effects of intron removal on base modification pattern of yeast tRNAPhe: an in vitro study. Nucleic Acids Res. 25 (1997) 2694-2701. [PMID: 9207014]

3. Strobel, M.C. and Abelson, J. Effect of intron mutations on processing and function of Saccharomyces cerevisiae SUP53 tRNA in vitro and in vivo. Mol. Cell Biol. 6 (1986) 2663-2673. [PMID: 3537724]

4. Walbott, H., Husson, C., Auxilien, S. and Golinelli-Pimpaneau, B. Cysteine of sequence motif VI is essential for nucleophilic catalysis by yeast tRNA m5C methyltransferase. RNA 13 (2007) 967-973. [PMID: 17475914]

[EC 2.1.1.202 created 1976 as EC 2.1.1.29, part transferred 2011 to EC 2.1.1.202]

EC 2.1.1.203

Accepted name: UDP-N-acetylbacillosamine N-acetyltransferase

Reaction: acetyl-CoA + UDP-N-acetylbacillosamine = CoA + UDP-N,N'-diacetylbacillosamine

For diagram of reaction click here.

Glossary: UDP-N-acetylbacillosamine = UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine
UDP-N,N'-diacetylbacillosamine = UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose

Other name(s): UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase; pglD (gene name)

Systematic name: acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase

Comments: The product, UDP-N,N'-diacetylbacillosamine, is an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-aspargine residues in Campylobacter species [1,2] and O-linked glycosylation of certain L-serine residues in Neisseria species [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry 45 (2006) 13659-13669. [PMID: 17087520]

2. Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. and Young, N.M. Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni. Biochemistry 47 (2008) 1827-1836. [PMID: 18198901]

3. Hartley, M.D., Morrison, M.J., Aas, F.E., Borud, B., Koomey, M. and Imperiali, B. Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N'-diacetylbacillosamine. Biochemistry 50 (2011) 4936-4948. [PMID: 21542610]

[EC 2.3.1.203 created 2012, modified 2013]

EC 2.1.1.204

Accepted name: RNA (cytosine38-C5)-methyltransferase

Reaction: S-adenosyl-L-methionine + cytosine38 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA

Other name(s): hDNMT2 (gene name); DNMT2 (gene name); TRDMT1 (gene name)

Systematic name: S-adenosyl-L-methionine:tRNA (cytosine38-C5)-methyltransferase

Comments: The eukaryotic enzyme catalyses methylation of cytosine38 in the anti-codon loop of tRNAAsp(GTC), tRNAVal(AAC) and tRNAGly(GCC). Methylation by Dnmt2 protects tRNAs against stress-induced cleavage by ribonuclease [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Goll, M.G., Kirpekar, F., Maggert, K.A., Yoder, J.A., Hsieh, C.L., Zhang, X., Golic, K.G., Jacobsen, S.E. and Bestor, T.H. Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2. Science 311 (2006) 395-398. [PMID: 16424344]

2. Jurkowski, T.P., Meusburger, M., Phalke, S., Helm, M., Nellen, W., Reuter, G. and Jeltsch, A. Human DNMT2 methylates tRNA(Asp) molecules using a DNA methyltransferase-like catalytic mechanism. RNA 14 (2008) 1663-1670. [PMID: 18567810]

3. Schaefer, M., Pollex, T., Hanna, K., Tuorto, F., Meusburger, M., Helm, M. and Lyko, F. RNA methylation by Dnmt2 protects transfer RNAs against stress-induced cleavage. Genes Dev. 24 (2010) 1590-1595. [PMID: 20679393]

[EC 2.1.1.204 created 1976 as EC 2.1.1.29, part transferred 2011 to EC 2.1.1.204]

EC 2.1.1.205

Accepted name: tRNA (cytidine32/guanosine34-2'-O)-methyltransferase

Reaction: S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O-methylguanosine34 in tRNA

Other name(s): Trm7p

Systematic name: S-adenosyl-L-methionine:tRNA (cytidine32/guanosine34-2'-O)-methyltransferase

Comments: The enzyme from Saccharomyces cerevisiae catalyses the formation of 2'-O-methylnucleotides at positions 32 and 34 of the yeast tRNAPhe, tRNATrp and, possibly, tRNALeu.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Pintard, L., Lecointe, F., Bujnicki, J.M., Bonnerot, C., Grosjean, H. and Lapeyre, B. Trm7p catalyses the formation of two 2'-O-methylriboses in yeast tRNA anticodon loop. EMBO J. 21 (2002) 1811-1820. [PMID: 11927565]

[EC 2.1.1.205 created 2011]

EC 2.1.1.206

Accepted name: tRNA (cytidine56-2'-O)-methyltransferase

Reaction: S-adenosyl-L-methionine + cytidine56 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA

Other name(s): aTrm56; tRNA ribose 2'-O-methyltransferase aTrm56; PAB1040 (gene name)

Systematic name: S-adenosyl-L-methionine:tRNA (cytidine56-2'-O)-methyltransferase

Comments: The archaeal enzyme specifically catalyses the S-adenosyl-L-methionine dependent 2'-O-ribose methylation of cytidine at position 56 in tRNA transcripts.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Renalier, M.H., Joseph, N., Gaspin, C., Thebault, P. and Mougin, A. The Cm56 tRNA modification in archaea is catalyzed either by a specific 2'-O-methylase, or a C/D sRNP. RNA 11 (2005) 1051-1063. [PMID: 15987815]

2. Kuratani, M., Bessho, Y., Nishimoto, M., Grosjean, H. and Yokoyama, S. Crystal structure and mutational study of a unique SpoU family archaeal methylase that forms 2'-O-methylcytidine at position 56 of tRNA. J. Mol. Biol. 375 (2008) 1064-1075. [PMID: 18068186]

[EC 2.1.1.206 created 2011]

EC 2.1.1.207

Accepted name: tRNA (cytidine34-2'-O)-methyltransferase

Reaction: (1) S-adenosyl-L-methionine + cytidine34 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNA
(2) S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNALeu = S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNALeu

Other name(s): yibK (gene name); methyltransferase yibK; TrmL; tRNA methyltransferase L; tRNA (cytidine34/5-carboxymethylaminomethyluridine34-2'-O)-methyltransferase

Systematic name: S-adenosyl-L-methionine:tRNA (cytidine34/5-carboxymethylaminomethyluridine34-2'-O)-methyltransferase

Comments: The enzyme from Escherichia coli catalyses the 2'-O-methylation of cytidine or 5-carboxymethylaminomethyluridine at the wobble position at nucleotide 34 in tRNALeuCmAA and tRNALeucmnm5UmAA. The enzyme is selective for the two tRNALeu isoacceptors and only methylates these when they present the correct anticodon loop sequence and modification pattern. Specifically, YibK requires a pyrimidine nucleoside at position 34, it has a clear preference for an adenosine at position 35, and it fails to methylate without prior addition of the N6-(isopentenyl)-2-methylthioadenosine modification at position 37.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Benitez-Paez, A., Villarroya, M., Douthwaite, S., Gabaldon, T. and Armengod, M.E. YibK is the 2'-O-methyltransferase TrmL that modifies the wobble nucleotide in Escherichia coli tRNA(Leu) isoacceptors. RNA 16 (2010) 2131-2143. [PMID: 20855540]

[EC 2.1.1.207 created 2011]

EC 2.1.1.208

Accepted name: 23S rRNA (uridine2479-2'-O)-methyltransferase

Reaction: S-adenosyl-L-methionine + uridine2479 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine2479 in 23S rRNA

Other name(s): AviRb

Systematic name: S-adenosyl-L-methionine:23S rRNA (uridine2479-2'-O)-methyltransferase

Comments: Streptomyces viridochromogenes produces the antibiotic avilamycin A which binds to the 50S ribosomal subunit to inhibit protein synthesis. To protect itself from the antibiotic, Streptomyces viridochromogenes utilizes two methyltransferases, 23S rRNA (uridine2479-2'-O)-methyltransferase and EC 2.1.1.209 [23S rRNA (guanine2535-N1)-methyltransferase], whose actions confer avilamycin resistance to the RNA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Mosbacher, T.G., Bechthold, A. and Schulz, G.E. Structure and function of the antibiotic resistance-mediating methyltransferase AviRb from Streptomyces viridochromogenes. J. Mol. Biol. 345 (2005) 535-545. [PMID: 15581897]

2. Treede, I., Jakobsen, L., Kirpekar, F., Vester, B., Weitnauer, G., Bechthold, A. and Douthwaite, S. The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA at the guanosine 2535 base and the uridine 2479 ribose. Mol. Microbiol. 49 (2003) 309-318. [PMID: 12828631]

3. Weitnauer, G., Gaisser, S., Trefzer, A., Stockert, S., Westrich, L., Quiros, L.M., Mendez, C., Salas, J.A. and Bechthold, A. An ATP-binding cassette transporter and two rRNA methyltransferases are involved in resistance to avilamycin in the producer organism Streptomyces viridochromogenes Tu57. Antimicrob. Agents Chemother. 45 (2001) 690-695. [PMID: 11181344]

[EC 2.1.1.208 created 2011]

EC 2.1.1.209

Accepted name: 23S rRNA (guanine2535-N1)-methyltransferase

Reaction: S-adenosyl-L-methionine + guanine2535 in 23S rRNA = S-adenosyl-L-homocysteine + N1-methylguanine2535 in 23S rRNA

Other name(s): AviRa

Systematic name: S-adenosyl-L-methionine:23S rRNA (guanine2535-N1)-methyltransferase

Comments: Streptomyces viridochromogenes produces the antibiotic avilamycin A which binds to the 50S ribosomal subunit to inhibit protein synthesis. To protect itself from the antibiotic, Streptomyces viridochromogenes utilizes two methyltransferases, 23S rRNA (guanine2535-N1)-methyltransferase and EC 2.1.1.208 [23S rRNA (uridine2479-2-O)-methyltransferase], whose actions confer avilamycin resistance to the RNA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Treede, I., Jakobsen, L., Kirpekar, F., Vester, B., Weitnauer, G., Bechthold, A. and Douthwaite, S. The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA at the guanosine 2535 base and the uridine 2479 ribose. Mol. Microbiol. 49 (2003) 309-318. [PMID: 12828631]

2. Weitnauer, G., Gaisser, S., Trefzer, A., Stockert, S., Westrich, L., Quiros, L.M., Mendez, C., Salas, J.A. and Bechthold, A. An ATP-binding cassette transporter and two rRNA methyltransferases are involved in resistance to avilamycin in the producer organism Streptomyces viridochromogenes Tu57. Antimicrob. Agents Chemother. 45 (2001) 690-695. [PMID: 11181344]

3. Mosbacher, T.G., Bechthold, A. and Schulz, G.E. Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes. J. Mol. Biol. 329 (2003) 147-157. [PMID: 12742024]

[EC 2.1.1.209 created 2011]

EC 2.1.1.210

Accepted name: demethylspheroidene O-methyltransferase

Reaction: S-adenosyl-L-methionine + demethylspheroidene = S-adenosyl-L-homocysteine + spheroidene

For diagram of reaction click here or click here

Other name(s): 1-hydroxycarotenoid O-methylase; 1-hydroxycarotenoid methylase; 1-HO-carotenoid methylase; CrtF

Systematic name: S-adenosyl-L-methionine:demethylspheroidene O-methyltransferase

Comments: In Rhodopseudomonas capsulata and Rubrivivax gelatinosus the enzyme is involved in biosynthesis of spheroidene [1,2,3]. In Rubrivivax gelatinosus the enzyme also catalyses the methylation of demethylspirilloxanthin to spirilloxanthin and the methylation of 3,4-didehydrorhodopin to anhydrorhodovibrin [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Badenhop, F., Steiger, S., Sandmann, M. and Sandmann, G. Expression and biochemical characterization of the 1-HO-carotenoid methylase CrtF from Rhodobacter capsulatus. FEMS Microbiol. Lett. 222 (2003) 237-242. [PMID: 12770713]

2. Pinta, V., Ouchane, S., Picaud, M., Takaichi, S., Astier, C. and Reiss-Husson, F. Characterization of unusual hydroxy- and ketocarotenoids in Rubrivivax gelatinosus: involvement of enzyme CrtF or CrtA. Arch. Microbiol. 179 (2003) 354-362. [PMID: 12664193]

3. Scolnik, P.A., Walker, M.A. and Marrs, B.L. Biosynthesis of carotenoids derived from neurosporene in Rhodopseudomonas capsulata. J. Biol. Chem. 255 (1980) 2427-2432. [PMID: 7358679]

[EC 2.1.1.210 created 2011]

EC 2.1.1.211

Accepted name: tRNASer (uridine44-2'-O)-methyltransferase

Reaction: S-adenosyl-L-methionine + uridine44 in tRNASer = S-adenosyl-L-homocysteine + 2'-O-methyluridine44 in tRNASer

For diagram of reaction click here.

Other name(s): TRM44

Systematic name: S-adenosyl-L-methionine:tRNASer (uridine44-2'-O)-methyltransferase

Comments: The 2'-O-methylation of uridine44 contributes to stability of tRNASer(CGA).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kotelawala, L., Grayhack, E.J. and Phizicky, E.M. Identification of yeast tRNA Um44 2'-O-methyltransferase (Trm44) and demonstration of a Trm44 role in sustaining levels of specific tRNASer species. RNA 14 (2008) 158-169. [PMID: 18025252]

[EC 2.1.1.211 created 2011]

EC 2.1.1.212

Accepted name: 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase

Reaction: S-adenosyl-L-methionine + 2,4',7-trihydroxyisoflavanone = S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone

For diagram of reaction click here.

Other name(s): SAM:2,4',7-trihydroxyisoflavanone 4'-O-methyltransferase; HI4'OMT; HMM1; MtIOMT5

Systematic name: S-adenosyl-L-methionine:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase

Comments: Specifically methylates 2,4',7-trihydroxyisoflavanone on the 4'-position. No activity with isoflavones [2]. The enzyme is involved in formononetin biosynthesis in legumes [1]. The protein from pea (Pisum sativum) also methylates (+)-6a-hydroxymaackiain at the 3-position (cf. EC 2.1.1.270, (+)-6a-hydroxymaackiain 3-O-methyltransferase) [4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Akashi, T., Sawada, Y., Shimada, N., Sakurai, N., Aoki, T. and Ayabe, S. cDNA cloning and biochemical characterization of S-adenosyl-L-methionine: 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase, a critical enzyme of the legume isoflavonoid phytoalexin pathway. Plant Cell Physiol. 44 (2003) 103-112. [PMID: 12610212]

2. Deavours, B.E., Liu, C.J., Naoumkina, M.A., Tang, Y., Farag, M.A., Sumner, L.W., Noel, J.P. and Dixon, R.A. Functional analysis of members of the isoflavone and isoflavanone O-methyltransferase enzyme families from the model legume Medicago truncatula. Plant Mol. Biol. 62 (2006) 715-733. [PMID: 17001495]

3. Liu, C.J., Deavours, B.E., Richard, S.B., Ferrer, J.L., Blount, J.W., Huhman, D., Dixon, R.A. and Noel, J.P. Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses. Plant Cell 18 (2006) 3656-3669. [PMID: 17172354]

4. Akashi, T., VanEtten, H.D., Sawada, Y., Wasmann, C.C., Uchiyama, H. and Ayabe, S. Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis. Phytochemistry 67 (2006) 2525-2530. [PMID: 17067644]

[EC 2.1.1.212 created 2011]

EC 2.1.1.213

Accepted name: tRNA (guanine10-N2)-dimethyltransferase

Reaction: 2 S-adenosyl-L-methionine + guanine10 in tRNA = 2 S-adenosyl-L-homocysteine + N2-dimethylguanine10 in tRNA (overall reaction)
(1a) S-adenosyl-L-methionine + guanine10 in tRNA = S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
(1b) S-adenosyl-L-methionine + N2-methylguanine10 in tRNA = S-adenosyl-L-homocysteine + N2-dimethylguanine10 in tRNA

Other name(s): PAB1283; N(2),N(2)-dimethylguanosine tRNA methyltransferase; Trm-G10; PabTrm-G10; PabTrm-m2 2G10 enzyme

Systematic name: S-adenosyl-L-methionine:tRNA (guanine10-N2)-dimethyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Armengaud, J., Urbonavicius, J., Fernandez, B., Chaussinand, G., Bujnicki, J.M. and Grosjean, H. N2-Methylation of guanosine at position 10 in tRNA is catalyzed by a THUMP domain-containing, S-adenosylmethionine-dependent methyltransferase, conserved in Archaea and Eukaryota. J. Biol. Chem. 279 (2004) 37142-37152. [PMID: 15210688]

[EC 2.1.1.213 created 2011 (EC 2.1.1.32 created 1972, part transferred 2011 to EC 2.1.1.213)]

EC 2.1.1.214

Accepted name: tRNA (guanine10-N2)-methyltransferase

Reaction: S-adenosyl-L-methionine + guanine10 in tRNA = S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA

Other name(s): (m2G10) methyltransferase; Trm11-Trm112 complex

Systematic name: S-adenosyl-L-methionine:tRNA (guanine10-N2)-methyltransferase

Comments: In contrast to the archaeal enzyme tRNA (guanine10-N2)-dimethyltransferase (EC 2.1.1.213), tRNA (guanine10-N2)-methyltransferase from yeast does not catalyse the methylation from N2-methylguanine10 to N2-dimethylguanine10 in tRNA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Purushothaman, S.K., Bujnicki, J.M., Grosjean, H. and Lapeyre, B. Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA. Mol. Cell Biol. 25 (2005) 4359-4370. [PMID: 15899842]

[EC 2.1.1.214 created 2011 (EC 2.1.1.32 created 1972, part transferred 2011 to EC 2.1.1.214)]

EC 2.1.1.215

Accepted name: tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase

Reaction: 4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA = 4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA

Other name(s): Trm1 (ambiguous); tRNA (N2,N2-guanine)-dimethyltransferase; tRNA (m2(2G26) methyltransferase; Trm1[tRNA (m2(2)G26) methyltransferase]

Systematic name: S-adenosyl-L-methionine:tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase

Comments: The enzyme from Aquifex aeolicus is similar to the TRM1 methyltransferases of archaea and eukarya (see EC 2.1.1.216, tRNA (guanine26-N2)-dimethyltransferase). However, it catalyses the double methylation of guanines at both positions 26 and 27 of tRNA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Awai, T., Kimura, S., Tomikawa, C., Ochi, A., Ihsanawati, Bessho, Y., Yokoyama, S., Ohno, S., Nishikawa, K., Yokogawa, T., Suzuki, T. and Hori, H. Aquifex aeolicus tRNA (N2,N2-guanine)-dimethyltransferase (Trm1) catalyzes transfer of methyl groups not only to guanine 26 but also to guanine 27 in tRNA. J. Biol. Chem. 284 (2009) 20467-20478. [PMID: 19491098]

[EC 2.1.1.215 created 2011 (EC 2.1.1.32 created 1972, part transferred 2011 to EC 2.1.1.215)]

EC 2.1.1.216

Accepted name: tRNA (guanine26-N2)-dimethyltransferase

Reaction: 2 S-adenosyl-L-methionine + guanine26 in tRNA = 2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA

Other name(s): Trm1p; TRM1; tRNA (m22G26)dimethyltransferase

Systematic name: S-adenosyl-L-methionine:tRNA (guanine26-N2)-dimethyltransferase

Comments: The enzyme dissociates from its tRNA substrate between the two consecutive methylation reactions. In contrast to EC 2.1.1.215, tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase, this enzyme does not catalyse the methylation of guanine27 in tRNA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Constantinesco, F., Motorin, Y. and Grosjean, H. Characterisation and enzymatic properties of tRNA(guanine26, N2,N2-dimethyltransferase (Trm1p) from Pyrococcus furiosus. J. Mol. Biol. 291 (1999) 375-392. [PMID: 10438627]

2. Constantinesco, F., Benachenhou, N., Motorin, Y. and Grosjean, H. The tRNA(guanine-26,N2-N2) methyltransferase (Trm1) from the hyperthermophilic archaeon Pyrococcus furiosus: cloning, sequencing of the gene and its expression in Escherichia coli. Nucleic Acids Res. 26 (1998) 3753-3761. [PMID: 9685492]

3. Liu, J., Liu, J. and Straby, K.B. Point and deletion mutations eliminate one or both methyl group transfers catalysed by the yeast TRM1 encoded tRNA (m22G26)dimethyltransferase. Nucleic Acids Res. 26 (1998) 5102-5108. [PMID: 9801306]

4. Liu, J., Zhou, G.Q. and Straby, K.B. Caenorhabditis elegans ZC376.5 encodes a tRNA (m22G26)dimethyltransferance in which 246arginine is important for the enzyme activity. Gene 226 (1999) 73-81. [PMID: 10048958]

[EC 2.1.1.216 created 2011 (EC 2.1.1.32 created 1972, part transferred 2011 to EC 2.1.1.216)]

EC 2.1.1.217

Accepted name: tRNA (adenine22-N1)-methyltransferase

Reaction: S-adenosyl-L-methionine + adenine22 in tRNA = S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA

Other name(s): TrmK; YqfN; Sp1610 (gene name); tRNA: m1A22 methyltransferase

Systematic name: S-adenosyl-L-methionine:tRNA (adenine22-N1)-methyltransferase

Comments: The enzyme specifically methylates adenine22 in tRNA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ta, H.M. and Kim, K.K. Crystal structure of Streptococcus pneumoniae Sp1610, a putative tRNA methyltransferase, in complex with S-adenosyl-L-methionine. Protein Sci. 19 (2010) 617-624. [PMID: 20052680]

2. Roovers, M., Kaminska, K.H., Tkaczuk, K.L., Gigot, D., Droogmans, L. and Bujnicki, J.M. The YqfN protein of Bacillus subtilis is the tRNA: m1A22 methyltransferase (TrmK). Nucleic Acids Res. 36 (2008) 3252-3262. [PMID: 18420655]

[EC 2.1.1.217 created 2011 (EC 2.1.1.36 created 1972, part transferred 2011 to EC 2.1.1.217)]

EC 2.1.1.218

Accepted name: tRNA (adenine9-N1)-methyltransferase

Reaction: S-adenosyl-L-methionine + adenine9 in tRNA = S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA

Other name(s): Trm10p (ambiguous); tRNA(m1G9/m1A9)-methyltransferase; tRNA(m1G9/m1A9)MTase; TK0422p (gene name); tRNA m1A9-methyltransferase; tRNA m1A9 Mtase

Systematic name: S-adenosyl-L-methionine:tRNA (adenine9-N1)-methyltransferase

Comments: The enzyme from Sulfolobus acidocaldarius specifically methylates adenine9 in tRNA [1]. The bifunctional enzyme from Thermococcus kodakaraensis also catalyses the methylation of guanine9 in tRNA (cf. EC 2.1.1.221, tRNA (guanine9-N1)-methyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kempenaers, M., Roovers, M., Oudjama, Y., Tkaczuk, K.L., Bujnicki, J.M. and Droogmans, L. New archaeal methyltransferases forming 1-methyladenosine or 1-methyladenosine and 1-methylguanosine at position 9 of tRNA. Nucleic Acids Res. 38 (2010) 6533-6543. [PMID: 20525789]

[EC 2.1.1.218 created 2011 (EC 2.1.1.36 created 1972, part transferred 2011 to EC 2.1.1.218)]

EC 2.1.1.219

Accepted name: tRNA (adenine57-N1/adenine58-N1)-methyltransferase

Reaction: 2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA = 2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA

Other name(s): TrmI; PabTrmI; AqTrmI; MtTrmI

Systematic name: S-adenosyl-L-methionine:tRNA (adenine57/adenine58-N1)-methyltransferase

Comments: The enzyme catalyses the formation of N1-methyladenine at two adjacent positions (57 and 58) in the T-loop of certain tRNAs (e.g. tRNAAsp). Methyladenosine at position 57 is an obligatory intermediate for the synthesis of methylinosine, which is commonly found at position 57 of archaeal tRNAs.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Roovers, M., Wouters, J., Bujnicki, J.M., Tricot, C., Stalon, V., Grosjean, H. and Droogmans, L. A primordial RNA modification enzyme: the case of tRNA (m1A) methyltransferase. Nucleic Acids Res. 32 (2004) 465-476. [PMID: 14739239]

2. Guelorget, A., Roovers, M., Guerineau, V., Barbey, C., Li, X. and Golinelli-Pimpaneau, B. Insights into the hyperthermostability and unusual region-specificity of archaeal Pyrococcus abyssi tRNA m1A57/58 methyltransferase. Nucleic Acids Res. 38 (2010) 6206-6218. [PMID: 20483913]

[EC 2.1.1.219 created 2011 (EC 2.1.1.36 created 1972, part transferred 2011 to EC 2.1.1.219)]

EC 2.1.1.220

Accepted name: tRNA (adenine58-N1)-methyltransferase

Reaction: S-adenosyl-L-methionine + adenine58 in tRNA = S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA

Other name(s): tRNA m1A58 methyltransferase; tRNA (m1A58) methyltransferase; TrmI; tRNA (m1A58) Mtase; Rv2118cp; Gcd10p-Gcd14p; Trm61p-Trm6p

Systematic name: S-adenosyl-L-methionine:tRNA (adenine58-N1)-methyltransferase

Comments: The enzyme specifically methylates adenine58 in tRNA. The methylation of A58 is critical for maintaining the stability of initiator tRNAMet in yeast [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Droogmans, L., Roovers, M., Bujnicki, J.M., Tricot, C., Hartsch, T., Stalon, V. and Grosjean, H. Cloning and characterization of tRNA (m1A58) methyltransferase (TrmI) from Thermus thermophilus HB27, a protein required for cell growth at extreme temperatures. Nucleic Acids Res. 31 (2003) 2148-2156. [PMID: 12682365]

2. Varshney, U., Ramesh, V., Madabushi, A., Gaur, R., Subramanya, H.S. and RajBhandary, U.L. Mycobacterium tuberculosis Rv2118c codes for a single-component homotetrameric m1A58 tRNA methyltransferase. Nucleic Acids Res. 32 (2004) 1018-1027. [PMID: 14960715]

3. Anderson, J., Phan, L. and Hinnebusch, A.G. The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-methyladenosine) methyltransferase of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 97 (2000) 5173-5178. [PMID: 10779558]

[EC 2.1.1.220 created 2011 (EC 2.1.1.36 created 1972, part transferred 2011 to EC 2.1.1.220)]

EC 2.1.1.221

Accepted name: tRNA (guanine9-N1)-methyltransferase

Reaction: S-adenosyl-L-methionine + guanine9 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA

Other name(s): Trm10p (ambiguous); tRNA(m1G9/m1A9)-methyltransferase; tRNA(m1G9/m1A9)MTase; tRNA (guanine-N(1)-)-methyltransferase; tRNA m1G9-methyltransferase; tRNA m1G9 MTase

Systematic name: S-adenosyl-L-methionine:tRNA (guanine9-N1)-methyltransferase

Comments: The enzyme from Saccharomyces cerevisiae specifically methylates guanine9 [1,2]. The bifunctional enzyme from Thermococcus kodakaraensis also catalyses the methylation of adenine9 in tRNA (cf. EC 2.1.1.218, tRNA (adenine9-N1)-methyltransferase) [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kempenaers, M., Roovers, M., Oudjama, Y., Tkaczuk, K.L., Bujnicki, J.M. and Droogmans, L. New archaeal methyltransferases forming 1-methyladenosine or 1-methyladenosine and 1-methylguanosine at position 9 of tRNA. Nucleic Acids Res. 38 (2010) 6533-6543. [PMID: 20525789]

2. Jackman, J.E., Montange, R.K., Malik, H.S. and Phizicky, E.M. Identification of the yeast gene encoding the tRNA m1G methyltransferase responsible for modification at position 9. RNA 9 (2003) 574-585. [PMID: 12702816]

[EC 2.1.1.221 created 2011 (EC 2.1.1.31 created 1971, part transferred 2011 to EC 2.1.1.221)]

EC 2.1.1.222

Accepted name: 2-polyprenyl-6-hydroxyphenol methylase

Reaction: S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol

For diagram of reaction, click here

Other name(s): ubiG (gene name, ambiguous); ubiG methyltransferase (ambiguous); 2-octaprenyl-6-hydroxyphenol methylase

Systematic name: S-adenosyl-L-methionine:3-(all-trans-polyprenyl)benzene-1,2-diol 2-O-methyltransferase

Comments: UbiG catalyses both methylation steps in ubiquinone biosynthesis in Escherichia coli. The second methylation is classified as EC 2.1.1.64 (3-demethylubiquinol 3-O-methyltransferase) [2]. In eukaryotes Coq3 catalyses the two methylation steps in ubiquinone biosynthesis. However, while the second methylation is common to both enzymes, the first methylation by Coq3 occurs at a different position within the pathway, and thus involves a different substrate and is classified as EC 2.1.1.114 (polyprenyldihydroxybenzoate methyltransferase). The substrate of the eukaryotic enzyme (3,4-dihydroxy-5-all-trans-polyprenylbenzoate) differs by an additional carboxylate moiety.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Poon, W.W., Barkovich, R.J., Hsu, A.Y., Frankel, A., Lee, P.T., Shepherd, J.N., Myles, D.C. and Clarke, C.F. Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis. J. Biol. Chem. 274 (1999) 21665-21672. [PMID: 10419476]

2. Hsu, A.Y., Poon, W.W., Shepherd, J.A., Myles, D.C. and Clarke, C.F. Complementation of coq3 mutant yeast by mitochondrial targeting of the Escherichia coli UbiG polypeptide: evidence that UbiG catalyzes both O-methylation steps in ubiquinone biosynthesis. Biochemistry 35 (1996) 9797-9806. [PMID: 8703953]

[EC 2.1.1.222 created 2011, modified 2013]

EC 2.1.1.223

Accepted name: tRNA1Val (adenine37-N6)-methyltransferase

Reaction: S-adenosyl-L-methionine + adenine37 in tRNA1Val = S-adenosyl-L-homocysteine + N6-methyladenine37 in tRNA1Val

Other name(s): YfiC

Systematic name: S-adenosyl-L-methionine:tRNA1Val (adenine37-N6)-methyltransferase

Comments: The enzyme specifically methylates adenine37 in tRNA1Val (anticodon cmo5UAC).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Golovina, A.Y., Sergiev, P.V., Golovin, A.V., Serebryakova, M.V., Demina, I., Govorun, V.M. and Dontsova, O.A. The yfiC gene of E. coli encodes an adenine-N6 methyltransferase that specifically modifies A37 of tRNA1Val(cmo5UAC). RNA 15 (2009) 1134-1141. [PMID: 19383770]

[EC 2.1.1.223 created 2011]

EC 2.1.1.224

Accepted name: 23S rRNA (adenine2503-C8)-methyltransferase

Reaction: 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin

Other name(s): Cfr (gene name)

Systematic name: S-adenosyl-L-methionine:23S rRNA (adenine2503-C8)-methyltransferase

Comments: This enzyme is a member of the ‘AdoMet radical’ (radical SAM) family. S-Adenosyl-L-methionine acts as both a radical generator and as the source of the appended methyl group. It contains an [4Fe-4S] cluster [3,6,7]. Cfr is an plasmid-acquired methyltransferase that protects cells from the action of antibiotics [1]. The enzyme methylates adenosine at position 2503 of 23S rRNA by a radical mechanism, transferring a CH2 group from S-adenosyl-L-methionine while retaining the hydrogen at the C-8 position of the adenine. RlmN first transfers an CH2 group to a conserved cysteine (Cys338 in Staphylococcus aureus) [7], the generated radical from a second S-adenosyl-L-methionine then attacks the methyl group, exctracting a hydrogen. The formed radical forms a covalent intermediate with the adenine group of the tRNA [8]. The enzyme will also methylate 2-methyladenine produced by the action of EC 2.1.1.192 [23S rRNA (adenine2503-C2)-methyltransferase].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Giessing, A.M., Jensen, S.S., Rasmussen, A., Hansen, L.H., Gondela, A., Long, K., Vester, B. and Kirpekar, F. Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria. RNA 15 (2009) 327-336. [PMID: 19144912]

2. Kaminska, K.H., Purta, E., Hansen, L.H., Bujnicki, J.M., Vester, B. and Long, K.S. Insights into the structure, function and evolution of the radical-SAM 23S rRNA methyltransferase Cfr that confers antibiotic resistance in bacteria. Nucleic Acids Res. 38 (2010) 1652-1663. [PMID: 20007606]

3. Yan, F., LaMarre, J.M., Röhrich, R., Wiesner, J., Jomaa, H., Mankin, A.S. and Fujimori, D.G. RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA. J. Am. Chem. Soc. 132 (2010) 3953-3964. [PMID: 20184321]

4. Yan, F. and Fujimori, D.G. RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift. Proc. Natl. Acad. Sci. USA 108 (2011) 3930-3934. [PMID: 21368151]

5. Grove, T.L., Benner, J.S., Radle, M.I., Ahlum, J.H., Landgraf, B.J., Krebs, C. and Booker, S.J. A radically different mechanism for S-adenosylmethionine-dependent methyltransferases. Science 332 (2011) 604-607. [PMID: 21415317]

6. Boal, A.K., Grove, T.L., McLaughlin, M.I., Yennawar, N.H., Booker, S.J. and Rosenzweig, A.C. Structural basis for methyl transfer by a radical SAM enzyme. Science 332 (2011) 1089-1092. [PMID: 21527678]

7. Grove, T.L., Radle, M.I., Krebs, C. and Booker, S.J. Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation. J. Am. Chem. Soc. 133 (2011) 19586-19589. [PMID: 21916495]

8. Grove, T.L., Livada, J., Schwalm, E.L., Green, M.T., Booker, S.J. and Silakov, A. A substrate radical intermediate in catalysis by the antibiotic resistance protein Cfr. Nat. Chem. Biol. 9 (2013) 422-427. [PMID: 23644479]

[EC 2.1.1.224 created 2011, modified 2014]

EC 2.1.1.225

Accepted name: tRNA:m4X modification enzyme

Reaction: (1) S-adenosyl-L-methionine + cytidine4 in tRNAPro = S-adenosyl-L-homocysteine + 2'-O-methylcytidine4 in tRNAPro
(2) S-adenosyl-L-methionine + cytidine4 in tRNAGly(GCC) = S-adenosyl-L-homocysteine + 2'-O-methylcytidine4 in tRNAGly(GCC)
(3) S-adenosyl-L-methionine + adenosine4 in tRNAHis = S-adenosyl-L-homocysteine + 2'-O-methyladenosine4 in tRNAHis

Other name(s): TRM13; Trm13p; tRNA:Xm4 modification enzyme

Systematic name: S-adenosyl-L-methionine:tRNAPro/His/Gly(GCC) (cytidine/adenosine4-2'-O)-methyltransferase

Comments: The enzyme from Saccharomyces cerevisiae 2'-O-methylates cytidine4 in tRNAPro and tRNAGly(GCC), and adenosine4 in tRNAHis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wilkinson, M.L., Crary, S.M., Jackman, J.E., Grayhack, E.J. and Phizicky, E.M. The 2'-O-methyltransferase responsible for modification of yeast tRNA at position 4. RNA 13 (2007) 404-413. [PMID: 17242307]

[EC 2.1.1.225 created 2011]

EC 2.1.1.226

Accepted name: 23S rRNA (cytidine1920-2'-O)-methyltransferase

Reaction: S-adenosyl-L-methionine + cytidine1920 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA

Other name(s): TlyA (ambiguous)

Systematic name: S-adenosyl-L-methionine:23S rRNA (cytidine1920-2'-O)-methyltransferase

Comments: The bifunctional enzyme from Mycobacterium tuberculosis 2'-O-methylates cytidine1920 in helix 69 of 23S rRNA and cytidine1409 in helix 44 of 16S rRNA (cf. EC 2.1.1.227, 16S rRNA (cytidine1409-2'-O)-methyltransferase). These methylations result in increased susceptibility to the antibiotics capreomycin and viomycin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Johansen, S.K., Maus, C.E., Plikaytis, B.B. and Douthwaite, S. Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2'-O-methylations in 16S and 23S rRNAs. Mol. Cell 23 (2006) 173-182. [PMID: 16857584]

2. Maus, C.E., Plikaytis, B.B. and Shinnick, T.M. Mutation of tlyA confers capreomycin resistance in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 49 (2005) 571-577. [PMID: 15673735]

[EC 2.1.1.226 created 2011]

EC 2.1.1.227

Accepted name: 16S rRNA (cytidine1409-2'-O)-methyltransferase

Reaction: S-adenosyl-L-methionine + cytidine1409 in 16S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine1409 in 16S rRNA

Other name(s): TlyA (ambiguous)

Systematic name: S-adenosyl-L-methionine:16S rRNA (cytidine1409-2'-O)-methyltransferase

Comments: The bifunctional enzyme from Mycobacterium tuberculosis 2'-O-methylates cytidine1409 in helix 44 of 16S rRNA and cytidine1920 in helix 69 of 23S rRNA (cf. EC 2.1.1.226, 23S rRNA (cytidine1920-2'-O)-methyltransferase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Johansen, S.K., Maus, C.E., Plikaytis, B.B. and Douthwaite, S. Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2'-O-methylations in 16S and 23S rRNAs. Mol. Cell 23 (2006) 173-182. [PMID: 16857584]

2. Maus, C.E., Plikaytis, B.B. and Shinnick, T.M. Mutation of tlyA confers capreomycin resistance in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 49 (2005) 571-577. [PMID: 15673735]

[EC 2.1.1.227 created 2011]

EC 2.1.1.228

Accepted name: tRNA (guanine37-N1)-methyltransferase

Reaction: S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA

For diagram of reaction click here.

Other name(s): TrmD; tRNA (m1G37) methyltransferase; transfer RNA (m1G37) methyltransferase; Trm5p; TRMT5; tRNA-(N1G37) methyltransferase; MJ0883 (gene name)

Systematic name: S-adenosyl-L-methionine:tRNA (guanine37-N1)-methyltransferase

Comments: This enzyme is important for the maintenance of the correct reading frame during translation. Unlike TrmD from Escherichia coli, which recognizes the G36pG37 motif preferentially, the human enzyme (encoded by TRMT5) also methylates inosine at position 37 [4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Takeda, H., Toyooka, T., Ikeuchi, Y., Yokobori, S., Okadome, K., Takano, F., Oshima, T., Suzuki, T., Endo, Y. and Hori, H. The substrate specificity of tRNA (m1G37) methyltransferase (TrmD) from Aquifex aeolicus. Genes Cells 11 (2006) 1353-1365. [PMID: 17121543]

2. Lee, C., Kramer, G., Graham, D.E. and Appling, D.R. Yeast mitochondrial initiator tRNA is methylated at guanosine 37 by the Trm5-encoded tRNA (guanine-N1-)-methyltransferase. J. Biol. Chem. 282 (2007) 27744-27753. [PMID: 17652090]

3. O'Dwyer, K., Watts, J.M., Biswas, S., Ambrad, J., Barber, M., Brule, H., Petit, C., Holmes, D.J., Zalacain, M. and Holmes, W.M. Characterization of Streptococcus pneumoniae TrmD, a tRNA methyltransferase essential for growth. J. Bacteriol. 186 (2004) 2346-2354. [PMID: 15060037]

4. Brule, H., Elliott, M., Redlak, M., Zehner, Z.E. and Holmes, W.M. Isolation and characterization of the human tRNA-(N1G37) methyltransferase (TRM5) and comparison to the Escherichia coli TrmD protein. Biochemistry 43 (2004) 9243-9255. [PMID: 15248782]

5. Goto-Ito, S., Ito, T., Ishii, R., Muto, Y., Bessho, Y. and Yokoyama, S. Crystal structure of archaeal tRNA(m(1)G37)methyltransferase aTrm5. Proteins 72 (2008) 1274-1289. [PMID: 18384044]

6. Ahn, H.J., Kim, H.W., Yoon, H.J., Lee, B.I., Suh, S.W. and Yang, J.K. Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition. EMBO J. 22 (2003) 2593-2603. [PMID: 12773376]

[EC 2.1.1.228 created 2011 (EC 2.1.1.31 created 1971, part transferred 2011 to EC 2.1.1.221)]

EC 2.1.1.229

Accepted name: tRNA (carboxymethyluridine34-5-O)-methyltransferase

Reaction: S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA = S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA

Glossary: 5-methoxycarboxymethyluridine = 5-(2-methoxy-2-oxoethyl)uridine

Other name(s): ALKBH8; ABH8; Trm9; tRNA methyltransferase 9

Systematic name: S-adenosyl-L-methionine:tRNA (carboxymethyluridine34-5-O)-methyltransferase

Comments: The enzyme catalyses the posttranslational modification of uridine residues at the wobble position 34 of the anticodon loop of tRNA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Fu, D., Brophy, J.A., Chan, C.T., Atmore, K.A., Begley, U., Paules, R.S., Dedon, P.C., Begley, T.J. and Samson, L.D. Human AlkB homolog ABH8 Is a tRNA methyltransferase required for wobble uridine modification and DNA damage survival. Mol. Cell Biol. 30 (2010) 2449-2459. [PMID: 20308323]

2. Songe-Moller, L., van den Born, E., Leihne, V., Vagbo, C.B., Kristoffersen, T., Krokan, H.E., Kirpekar, F., Falnes, P.O. and Klungland, A. Mammalian ALKBH8 possesses tRNA methyltransferase activity required for the biogenesis of multiple wobble uridine modifications implicated in translational decoding. Mol. Cell Biol. 30 (2010) 1814-1827. [PMID: 20123966]

3. Kalhor, H.R. and Clarke, S. Novel methyltransferase for modified uridine residues at the wobble position of tRNA. Mol. Cell Biol. 23 (2003) 9283-9292. [PMID: 14645538]

[EC 2.1.1.229 created 2011]

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, CAS registry number:

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. [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. [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 reaction, click here

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, CAS registry number:

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. [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 reaction, click here

Glossary: naringenin = (2S)-5,7,4'-trihydroxyflavanone = (2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-2,3-dihydrochromen-4-one
sakuranetin = (2S)-5,4'-dihydroxy-7-methoxyflavanone = (2S)-5-hydroxy-2-(4-hydroxyphenyl)-7-methoxy-2,3-dihydrochromen-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 Oryza sativa against pathogen attack.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

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. [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, PDB, CAS registry number:

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. [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. [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 reaction 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, PDB, CAS registry number:

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. [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. [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

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, PDB, CAS registry number:

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. [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. [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 reaction 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, CAS registry number:

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. [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 reaction 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, CAS registry number:

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. [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 reaction 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, PDB, CAS registry number:

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. [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, CAS registry number:

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. [PMID: 11514520]

[EC 2.1.1.239 created 2012]

EC 2.1.1.240

Accepted name: trans-resveratrol di-O-methyltransferase

Reaction: 2 S-adenosyl-L-methionine + trans-resveratrol = 2 S-adenosyl-L-homocysteine + pterostilbene (overall reaction)
(1a) S-adenosyl-L-methionine + trans-resveratrol = S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene
(1b) S-adenosyl-L-methionine + 3-methoxy-4',5-dihydroxy-trans-stilbene = S-adenosyl-L-homocysteine + pterostilbene

For diagram of reaction click here.

Glossary: 3-methoxy-4',5-dihydroxy-trans-stilbene = resveratrol monomethyl ether
pterostilbene = 3,5-dimethoxy-4'-hydroxy-trans-stilbene
trans-resveratrol = 3,4',5-trihydroxy-trans-stilbene

Other name(s): ROMT; resveratrol O-methyltransferase; pterostilbene synthase

Systematic name: S-adenosyl-L-methionine:trans-resveratrol 3,5-O-dimethyltransferase

Comments: The enzyme catalyses the biosynthesis of pterostilbene from resveratrol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Schmidlin, L., Poutaraud, A., Claudel, P., Mestre, P., Prado, E., Santos-Rosa, M., Wiedemann-Merdinoglu, S., Karst, F., Merdinoglu, D. and Hugueney, P. A stress-inducible resveratrol O-methyltransferase involved in the biosynthesis of pterostilbene in grapevine. Plant Physiol. 148 (2008) 1630-1639. [PMID: 18799660]

[EC 2.1.1.240 created 2012]

EC 2.1.1.241

Accepted name: 2,4,7-trihydroxy-1,4-benzoxazin-3-one-glucoside 7-O-methyltransferase

Reaction: S-adenosyl-L-methionine + (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = S-adenosyl-L-homocysteine + (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside

For diagram of reaction click here.

Glossary: (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = TRIMBOA β-D-glucoside
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIMBOA β-D-glucoside

Other name(s): BX7 (gene name); OMT BX7

Systematic name: S-adenosyl-L-methionine:(2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside 7-O-methyltransferase

Comments: The enzyme is involved in the biosynthesis of the protective and allelophatic benzoxazinoid DIMBOA [(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin] in some plants, most commonly from the family of Poaceae (grasses).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Jonczyk, R., Schmidt, H., Osterrieder, A., Fiesselmann, A., Schullehner, K., Haslbeck, M., Sicker, D., Hofmann, D., Yalpani, N., Simmons, C., Frey, M. and Gierl, A. Elucidation of the final reactions of DIMBOA-glucoside biosynthesis in maize: characterization of Bx6 and Bx7. Plant Physiol. 146 (2008) 1053-1063. [PMID: 18192444]

[EC 2.1.1.241 created 2012]

EC 2.1.1.242

Accepted name: 16S rRNA (guanine1516-N2)-methyltransferase

Reaction: S-adenosyl-L-methionine + guanine1516 in 16S rRNA = S-adenosyl-L-homocysteine + N2-methylguanine1516 in 16S rRNA

Other name(s): yhiQ (gene name); rsmJ (gene name); m2G1516 methyltransferase

Systematic name: S-adenosyl-L-methionine:16S rRNA (guanine1516-N2)-methyltransferase

Comments: The enzyme specifically methylates guanine1516 at N2 in 16S rRNA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Basturea, G.N., Dague, D.R., Deutscher, M.P. and Rudd, K.E. YhiQ Is RsmJ, the Methyltransferase Responsible for Methylation of G1516 in 16S rRNA of E. coli. J. Mol. Biol. 415 (2012) 16-21. [PMID: 22079366]

[EC 2.1.1.242 created 2012]

EC 2.1.1.243

Accepted name: 2-ketoarginine methyltransferase

Reaction: S-adenosyl-L-methionine + 5-guanidino-2-oxopentanoate = S-adenosyl-L-homocysteine + 5-guanidino-3-methyl-2-oxopentanoate

Glossary: 5-guanidino-2-oxopentanoate = 2-ketoarginine
5-guanidino-3-methyl-2-oxopentanoate = 5-carbamimidamido-3-methyl-2-oxopentanoate

Other name(s): mrsA (gene name)

Systematic name: S-adenosyl-L-methionine:5-carbamimidamido-2-oxopentanoate S-methyltransferase

Comments: The enzyme is involved in production of the rare amino acid 3-methylarginine, which is used by the epiphytic bacterium Pseudomonas syringae pv. syringae as an antibiotic against the related pathogenic species Pseudomonas syringae pv. glycinea.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Braun, S.D., Hofmann, J., Wensing, A., Ullrich, M.S., Weingart, H., Völksch, B. and Spiteller, D. Identification of the biosynthetic gene cluster for 3-methylarginine, a toxin produced by Pseudomonas syringae pv. syringae 22d/93. Appl. Environ. Microbiol. 76 (2010) 2500-2508. [PMID: 20190091]

[EC 2.1.1.243 created 2012]

EC 2.1.1.244

Accepted name: protein N-terminal methyltransferase

Reaction: (1) 3 S-adenosyl-L-methionine + N-terminal-(A,S)PK-[protein] = 3 S-adenosyl-L-homocysteine + N-terminal-N,N,N-trimethyl-N-(A,S)PK-[protein] (overall reaction)
(1a) S-adenosyl-L-methionine + N-terminal-(A,S)PK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-(A,S)PK-[protein]
(1b) S-adenosyl-L-methionine + N-terminal-N-methyl-N-(A,S)PK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-(A,S)PK-[protein]
(1c) S-adenosyl-L-methionine + N-terminal-N,N-dimethyl-N-(A,S)PK-serine-[protein] = S-adenosyl-L-homocysteine + N-terminal-N,N,N-trimethyl-N-(A,S)PK-[protein]
(2) 2 S-adenosyl-L-methionine + N-terminal-PPK-[protein] = 2 S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-PPK-[protein] (overall reaction)
(2a) S-adenosyl-L-methionine + N-terminal-PPK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-PPK-[protein]
(2b) S-adenosyl-L-methionine + N-terminal-N-methyl-N-PPK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-PPK-[protein]

Other name(s): NMT1 (gene name); METTL11A (gene name)

Systematic name: S-adenosyl-L-methionine:N-terminal-(A,P,S)PK-[protein] methyltransferase

Comments: This enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. When the terminal amino acid is L-proline, the enzyme catalyses two successive methylations of its α-amino group. When the first amino acid is either L-alanine or L-serine, the enzyme catalyses three successive methylations. The Pro-Lys in positions 2-3 cannot be exchanged for other amino acids [1,2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Webb, K.J., Lipson, R.S., Al-Hadid, Q., Whitelegge, J.P. and Clarke, S.G. Identification of protein N-terminal methyltransferases in yeast and humans. Biochemistry 49 (2010) 5225-5235. [PMID: 20481588]

2. Tooley, C.E., Petkowski, J.J., Muratore-Schroeder, T.L., Balsbaugh, J.L., Shabanowitz, J., Sabat, M., Minor, W., Hunt, D.F. and Macara, I.G. NRMT is an α-N-methyltransferase that methylates RCC1 and retinoblastoma protein. Nature 466 (2010) 1125-1128. [PMID: 20668449]

[EC 2.1.1.244 created 2012]

EC 2.1.1.245

Accepted name: 5-methyltetrahydrosarcinapterin:corrinoid—iron-sulfur protein Co-methyltransferase

Reaction: a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrosarcinapterin = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrosarcinapterin

Other name(s): cdhD (gene name); cdhE (gene name)

Systematic name: 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein methyltransferase

Comments: Catalyses the transfer of a methyl group from the cobamide cofactor of a corrinoid/Fe-S protein to the N5 group of tetrahydrosarcinapterin. Forms, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, the acetyl-CoA decarbonylase/synthase complex that catalyses the demethylation of acetyl-CoA in a reaction that also forms CO2. This reaction is a key step in methanogenesis from acetate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Maupin-Furlow, J. and Ferry, J.G. Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila. J. Bacteriol. 178 (1996) 340-346. [PMID: 8550451]

2. Grahame, D.A. and DeMoll, E. Partial reactions catalyzed by protein components of the acetyl-CoA decarbonylase synthase enzyme complex from Methanosarcina barkeri. J. Biol. Chem. 271 (1996) 8352-8358. [PMID: 8626532]

[EC 2.1.1.245 created 2012]

EC 2.1.1.246

Accepted name: [methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase

Reaction: a [methyl-Co(III) methanol-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methanol-specific corrinoid protein]

Glossary: CoM = coenzyme M = 2-mercaptoethanesulfonate

Other name(s): methyltransferase 2 (ambiguous); mtaA (gene name)

Systematic name: methylated methanol-specific corrinoid protein:Coenzyme M methyltransferase

Comments: The enzyme, which is involved in methanogenesis from methanol, catalyses the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.90, methanol—corrinoid protein Co-methyltransferase), where it is bound to the cobalt cofactor, to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis. Free methylcob(I)alamin can substitute for the corrinoid protein in vitro [5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. LeClerc, G.M. and Grahame, D.A. Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression. J. Biol. Chem. 271 (1996) 18725-18731. [PMID: 8702528]

2. Harms, U. and Thauer, R.K. Methylcobalamin: coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli. Eur. J. Biochem. 235 (1996) 653-659. [PMID: 8654414]

3. Sauer, K. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Zinc dependence and thermodynamics of the methanol:cob(I)alamin methyltransferase reaction. Eur. J. Biochem. 249 (1997) 280-285. [PMID: 9363780]

4. Sauer, K., Harms, U. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties and encoding genes of the corrinoid protein MT1. Eur. J. Biochem. 243 (1997) 670-677. [PMID: 9057830]

5. Sauer, K. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri – substitution of the corrinoid harbouring subunit MtaC by free cob(I)alamin. Eur. J. Biochem. 261 (1999) 674-681. [PMID: 10215883]

[EC 2.1.1.246 created 2012]

EC 2.1.1.247

Accepted name: [methyl-Co(III) methylamine-specific corrinoid protein]—coenzyme M methyltransferase

Reaction: a [methyl-Co(III) methylamine-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]

Glossary: CoM = coenzyme M = 2-mercaptoethanesulfonate

Other name(s): methyltransferase 2 (ambiguous); MT2 (ambiguous); MT2-A; mtbA (gene name)

Systematic name: methylated monomethylamine-specific corrinoid protein:Coenzyme M methyltransferase

Comments: Contains zinc [2]. The enzyme, which is involved in methanogenesis from mono-, di-, and trimethylamine, catalyses the transfer of a methyl group bound to the cobalt cofactor of several corrinoid proteins (mono-, di-, and trimethylamine-specific corrinoid proteins (cf. EC 2.1.1.248, methylamine—corrinoid protein Co-methyltransferase, EC 2.1.1.249, dimethylamine—corrinoid protein Co-methyltransferase, and EC 2.1.1.250, trimethylamine—corrinoid protein Co-methyltransferase) to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Burke, S.A. and Krzycki, J.A. Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine. J. Bacteriol. 177 (1995) 4410-4416. [PMID: 7635826]

2. LeClerc, G.M. and Grahame, D.A. Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression. J. Biol. Chem. 271 (1996) 18725-18731. [PMID: 8702528]

3. Ferguson, D.J., Jr. and Krzycki, J.A. Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri. J. Bacteriol. 179 (1997) 846-852. [PMID: 9006042]

4. Burke, S.A., Lo, S.L. and Krzycki, J.A. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J. Bacteriol. 180 (1998) 3432-3440. [PMID: 9642198]

5. Ferguson, D.J., Jr., Gorlatova, N., Grahame, D.A. and Krzycki, J.A. Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 275 (2000) 29053-29060. [PMID: 10852929]

[EC 2.1.1.247 created 2012]

EC 2.1.1.248

Accepted name: methylamine—corrinoid protein Co-methyltransferase

Reaction: methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + NH3

Other name(s): mtmB (gene name); monomethylamine methyltransferase

Systematic name: monomethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase

Comments: The enzyme, which catalyses the transfer of a methyl group from methylamine to a methylamine-specific corrinoid protein (MtmC), is involved in methanogenesis from methylamine. The enzyme contains the unusual amino acid pyrrolysine [3]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Burke, S.A. and Krzycki, J.A. Reconstitution of Monomethylamine:Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 272 (1997) 16570-16577. [PMID: 9195968]

2. Burke, S.A., Lo, S.L. and Krzycki, J.A. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J. Bacteriol. 180 (1998) 3432-3440. [PMID: 9642198]

3. Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484-491. [PMID: 15450490]

[EC 2.1.1.248 created 2012]

EC 2.1.1.249

Accepted name: dimethylamine—corrinoid protein Co-methyltransferase

Reaction: dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein] = a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine

Other name(s): mtbB (gene name); dimethylamine methyltransferase

Systematic name: dimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase

Comments: The enzyme, which catalyses the transfer of a methyl group from dimethylamine to a dimethylamine-specific corrinoid protein (MtbC), is involved in methanogenesis from dimethylamine. The enzyme contains the unusual amino acid pyrrolysine [3]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wassenaar, R.W., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and characterization of dimethylamine:5-hydroxybenzimidazolyl-cobamide methyltransferase from Methanosarcina barkeri Fusaro. Eur. J. Biochem. 253 (1998) 692-697. [PMID: 9654067]

2. Ferguson, D.J., Jr., Gorlatova, N., Grahame, D.A. and Krzycki, J.A. Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 275 (2000) 29053-29060. [PMID: 10852929]

3. Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484-491. [PMID: 15450490]

[EC 2.1.1.249 created 2012]

EC 2.1.1.250

Accepted name: trimethylamine—corrinoid protein Co-methyltransferase

Reaction: trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] = a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine

Other name(s): mttB (gene name); trimethylamine methyltransferase

Systematic name: trimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase

Comments: The enzyme, which catalyses the transfer of a methyl group from trimethylamine to a trimethylamine-specific corrinoid protein (MttC), is involved in methanogenesis from trimethylamine. The enzyme contains the unusual amino acid pyrrolysine [2]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ferguson, D.J., Jr. and Krzycki, J.A. Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri. J. Bacteriol. 179 (1997) 846-852. [PMID: 9006042]

2. Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484-491. [PMID: 15450490]

[EC 2.1.1.250 created 2012]


Continued with EC 2.1.1.251 to EC 2.1.1.307
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