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
EC 2.1.1.201 to EC 2.1.1.250
EC 2.1.1.251 to EC 2.1.1.300

Contents

EC 2.1.1.301 cypemycin N-terminal methyltransferase
EC 2.1.1.302 3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase
EC 2.1.1.303 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase
EC 2.1.1.304 L-tyrosine C3-methyltransferase
EC 2.1.1.305 8-demethyl-8-α-L-rhamnosyltetracenomycin-C 2'-O-methyltransferase
EC 2.1.1.306 8-demethyl-8-(2-methoxy-α-L-rhamnosyl)tetracenomycin-C 3'-O-methyltransferase
EC 2.1.1.307 8-demethyl-8-(2,3-dimethoxy-α-L-rhamnosyl)tetracenomycin-C 4'-O-methyltransferase
EC 2.1.1.308 cytidylyl-2-hydroxyethylphosphonate methyltransferase
EC 2.1.1.309 18S rRNA (guanine1575-N7)-methyltransferase
EC 2.1.1.310 25S rRNA (cytosine2870-C5)-methyltransferase
EC 2.1.1.311 25S rRNA (cytosine2278-C5)-methyltransferase
EC 2.1.1.312 25S rRNA (uracil2843-N3)-methyltransferase
EC 2.1.1.313 25S rRNA (uracil2634-N3)-methyltransferase
EC 2.1.1.314 diphthine methyl ester synthase
EC 2.1.1.315 27-O-demethylrifamycin SV methyltransferase
EC 2.1.1.316 mitomycin 6-O-methyltransferase
EC 2.1.1.317 sphingolipid C9-methyltransferase
EC 2.1.1.318 [trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase
EC 2.1.1.319 type I protein arginine methyltransferase
EC 2.1.1.320 type II protein arginine methyltransferase
EC 2.1.1.321 type III protein arginine methyltransferase
EC 2.1.1.322 type IV protein arginine methyltransferase
EC 2.1.1.323 (–)-pluviatolide 4-O-methyltransferase
EC 2.1.1.324 dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase
EC 2.1.1.325 juvenile hormone-III synthase
EC 2.1.1.326 N-acetyl-demethylphosphinothricin P-methyltransferase
EC 2.1.1.327 phenazine-1-carboxylate N-methyltransferase
EC 2.1.1.328 N-demethylindolmycin N-methyltransferase
EC 2.1.1.329 demethylphylloquinol methyltransferase
EC 2.1.1.330 5'-demethylyatein 5'-O-methyltransferase
EC 2.1.1.331 bacteriochlorophyllide d C-121-methyltransferase
EC 2.1.1.332 bacteriochlorophyllide d C-82-methyltransferase
EC 2.1.1.333 bacteriochlorophyllide d C-20 methyltransferase
EC 2.1.1.334 methanethiol S-methyltransferase
EC 2.1.1.335 4-amino-anhydrotetracycline N4-methyltransferase
EC 2.1.1.336 norbelladine O-methyltransferase
EC 2.1.1.337 reticuline N-methyltransferase
EC 2.1.1.338 desmethylxanthohumol 6'-O-methyltransferase
EC 2.1.1.339 xanthohumol 4'-O-methyltransferase
EC 2.1.1.340 3-aminomethylindole N-methyltransferase
EC 2.1.1.341 vanillate/3-O-methylgallate O-demethylase
EC 2.1.1.342 anaerobilin synthase
EC 2.1.1.343 8-amino-8-demethylriboflavin N,N-dimethyltransferase
EC 2.1.1.344 ornithine lipid N-methyltransferase
EC 2.1.1.345 psilocybin synthase
EC 2.1.1.346 U6 snRNA m6A methyltransferase
EC 2.1.1.347 (+)-O-methylkolavelool synthase
EC 2.1.1.348 mRNA m6A methyltransferase
EC 2.1.1.349 toxoflavin synthase
EC 2.1.1.350 menaquinone C8-methyltransferase
EC 2.1.1.351 nocamycin O-methyltransferase
EC 2.1.1.352 3-O-acetyl-4′-O-demethylpapaveroxine 4′-O-methyltransferase
EC 2.1.1.353 demethylluteothin O-methyltransferase
EC 2.1.1.354 histone H3 lysine4 N-trimethyltransferase
EC 2.1.1.355 histone H3 lysine9 N-trimethyltransferase
EC 2.1.1.356 histone H3 lysine27 N-trimethyltransferase
EC 2.1.1.357 histone H3 lysine36 N-dimethyltransferase
EC 2.1.1.358 histone H3 dimethyl-L-lysine36 N-methyltransferase
EC 2.1.1.359 histone H3 lysine36 N-trimethyltransferase
EC 2.1.1.360 histone H3 lysine79 N-trimethyltransferase
EC 2.1.1.361 histone H4 lysine20 N-methyltransferase
EC 2.1.1.362 histone H4 N-methyl-L-lysine20 N-methyltransferase
EC 2.1.1.363 pre-sodorifen synthase

Entries

EC 2.1.1.301

Accepted name: cypemycin N-terminal methyltransferase

Reaction: 2 S-adenosyl-L-methionine + N-terminal L-alanine-[cypemycin] = 2 S-adenosyl-L-homocysteine + N-terminal N,N-dimethyl-L-alanine-[cypemycin]

Other name(s): CypM

Systematic name: S-adenosyl-L-methionine:N-terminal L-alanine-[cypemycin] N-methyltransferase

Comments: The enzyme, isolated from the bacterium Streptomyces sp. OH-4156, can methylate a variety of linear oligopeptides, cyclic peptides such as nisin and haloduracin, and the ε-amino group of lysine [2]. Cypemycin is a peptide antibiotic, a member of the linaridins, a class of posttranslationally modified ribosomally synthesized peptides.

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

References:

1. Claesen, J. and Bibb, M. Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides. Proc. Natl. Acad. Sci. USA 107 (2010) 16297-16302. [PMID: 20805503]

2. Zhang, Q. and van der Donk, W.A. Catalytic promiscuity of a bacterial α-N-methyltransferase. FEBS Lett 586 (2012) 3391-3397. [PMID: 22841713]

[EC 2.1.1.301 created 2014]

EC 2.1.1.302

Accepted name: 3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase

Reaction: S-adenosyl-L-methionine + 3-hydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 3-methoxy-5-methyl-1-naphthoate

For diagram of reaction click here.

Other name(s): AziB2

Systematic name: S-adenosyl-L-methionine:3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase

Comments: The enzyme from the bacterium Streptomyces sahachiroi is involved in the biosynthesis of 3-methoxy-5-methyl-1-naphthoate, a component of of the the antitumor antibiotic azinomycin B.

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

References:

1. Ding, W., Deng, W., Tang, M., Zhang, Q., Tang, G., Bi, Y. and Liu, W. Biosynthesis of 3-methoxy-5-methyl naphthoic acid and its incorporation into the antitumor antibiotic azinomycin B. Mol. Biosyst. 6 (2010) 1071-1081. [PMID: 20485749]

[EC 2.1.1.302 created 2014]

EC 2.1.1.303

Accepted name: 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase

Reaction: S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate

For diagram of reaction click here.

Other name(s): NcsB1; neocarzinostatin O-methyltransferase

Systematic name: S-adenosyl-L-methionine:2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase

Comments: The enzyme from the bacterium Streptomyces carzinostaticus is involved in the biosynthesis of 2-hydroxy-7-methoxy-5-methyl-1-naphthoate. This compound is part of the enediyne chromophore of the antitumor antibiotic neocarzinostatin. In vivo the enzyme catalyses the regiospecific methylation at the 7-hydroxy group of its native substrate 2,7-dihydroxy-5-methyl-1-naphthoate. In vitro it also recognizes other dihydroxynaphthoic acids and catalyses their regiospecific O-methylation.

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

References:

1. Luo, Y., Lin, S., Zhang, J., Cooke, H.A., Bruner, S.D. and Shen, B. Regiospecific O-methylation of naphthoic acids catalyzed by NcsB1, an O-methyltransferase involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. J. Biol. Chem. 283 (2008) 14694-14702. [PMID: 18387946]

2. Cooke, H.A., Guenther, E.L., Luo, Y., Shen, B. and Bruner, S.D. Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. Biochemistry 48 (2009) 9590-9598. [PMID: 19702337]

[EC 2.1.1.303 created 2014]

EC 2.1.1.304

Accepted name: L-tyrosine C3-methyltransferase

Reaction: S-adenosyl-L-methionine + L-tyrosine = S-adenosyl-L-homocysteine + 3-methyl-L-tyrosine

For diagram of reaction click here.

Other name(s): SfmM2; SacF

Systematic name: S-adenosyl-L-methionine:L-tyrosine C3-methyltransferase

Comments: The enzyme from the bacterium Streptomyces lavendulae is involved in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family.

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

References:

1. Tang, M.C., Fu, C.Y. and Tang, G.L. Characterization of SfmD as a heme peroxidase that catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyltyrosine in saframycin A biosynthesis. J. Biol. Chem. 287 (2012) 5112-5121. [PMID: 22187429]

[EC 2.1.1.304 created 2014]

EC 2.1.1.305

Accepted name: 8-demethyl-8-α-L-rhamnosyltetracenomycin-C 2'-O-methyltransferase

Reaction: S-adenosyl-L-methionine + 8-demethyl-8-α-L-rhamnosyltetracenomycin C = S-adenosyl-L-homocysteine + 8-demethyl-8-(2-O-methyl-α-L-rhamnosyl)tetracenomycin C

For diagram of reaction click here.

Glossary: 8-demethyl-8-α-L-rhamnosyltetracenomycin C = methyl (6aR,7S,10aR)-6a,7,10a,12-tetrahydroxy-8-methoxy-1-methyl-6,10,11-trioxo-3-α-L-rhamnosyloxy-6,6a,7,10,10a,11-hexahydrotetracene-2-carboxylate

Other name(s): ElmMI

Systematic name: S-adenosyl-L-methionine:8-demethyl-8-α-L-rhamnosyltetracenomycin-C 2'-O-methyltransferase

Comments: The enzyme from the bacterium Streptomyces olivaceus is involved in the biosynthesis of the polyketide elloramycin.

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

References:

1. Patallo, E.P., Blanco, G., Fischer, C., Brana, A.F., Rohr, J., Mendez, C. and Salas, J.A. Deoxysugar methylation during biosynthesis of the antitumor polyketide elloramycin by Streptomyces olivaceus. Characterization of three methyltransferase genes. J. Biol. Chem. 276 (2001) 18765-18774. [PMID: 11376004]

[EC 2.1.1.305 created 2014]

EC 2.1.1.306

Accepted name: 8-demethyl-8-(2-methoxy-α-L-rhamnosyl)tetracenomycin-C 3'-O-methyltransferase

Reaction: S-adenosyl-L-methionine + 8-demethyl-8-(2-O-methyl-α-L-rhamnosyl)tetracenomycin C = S-adenosyl-L-homocysteine + 8-demethyl-8-(2,3-di-O-methyl-α-L-rhamnosyl)tetracenomycin C

For diagram of reaction click here.

Glossary: 8-demethyl-8-α-L-rhamnosyltetracenomycin C = methyl (6aR,7S,10aR)-6a,7,10a,12-tetrahydroxy-8-methoxy-1-methyl-6,10,11-trioxo-3-α-L-rhamnosyloxy-6,6a,7,10,10a,11-hexahydrotetracene-2-carboxylate

Other name(s): ElmMII

Systematic name: S-adenosyl-L-methionine:8-demethyl-8-(2-methoxy-α-L-rhamnosyl)tetracenomycin-C 3'-O-methyltransferase

Comments: The enzyme from the bacterium Streptomyces olivaceus is involved in the biosynthesis of the polyketide elloramycin.

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

References:

1. Patallo, E.P., Blanco, G., Fischer, C., Brana, A.F., Rohr, J., Mendez, C. and Salas, J.A. Deoxysugar methylation during biosynthesis of the antitumor polyketide elloramycin by Streptomyces olivaceus. Characterization of three methyltransferase genes. J. Biol. Chem. 276 (2001) 18765-18774. [PMID: 11376004]

[EC 2.1.1.306 created 2014]

EC 2.1.1.307

Accepted name: 8-demethyl-8-(2,3-dimethoxy-α-L-rhamnosyl)tetracenomycin-C 4'-O-methyltransferase

Reaction: S-adenosyl-L-methionine + 8-demethyl-8-(2,3-di-O-methyl-α-L-rhamnosyl)tetracenomycin C = S-adenosyl-L-homocysteine + 8-demethyl-8-(2,3,4-tri-O-methyl-α-L-rhamnosyl)tetracenomycin C

For diagram of reaction click here.

Glossary: 8-demethyl-8-α-L-rhamnosyltetracenomycin C = methyl (6aR,7S,10aR)-6a,7,10a,12-tetrahydroxy-8-methoxy-1-methyl-6,10,11-trioxo-3-α-L-rhamnosyloxy-6,6a,7,10,10a,11-hexahydrotetracene-2-carboxylate

Other name(s): ElmMIII

Systematic name: S-adenosyl-L-methionine:8-demethyl-8-(2,3-di-O-methoxy-α-L-rhamnosyl)tetracenomycin-C 4'-O-methyltransferase

Comments: The enzyme from the bacterium Streptomyces olivaceus is involved in the biosynthesis of the polyketide elloramycin.

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

References:

1. Patallo, E.P., Blanco, G., Fischer, C., Brana, A.F., Rohr, J., Mendez, C. and Salas, J.A. Deoxysugar methylation during biosynthesis of the antitumor polyketide elloramycin by Streptomyces olivaceus. Characterization of three methyltransferase genes. J. Biol. Chem. 276 (2001) 18765-18774. [PMID: 11376004]

[EC 2.1.1.307 created 2014]

EC 2.1.1.308

Accepted name: cytidylyl-2-hydroxyethylphosphonate methyltransferase

Reaction: 2 S-adenosyl-L-methionine + cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} + reduced acceptor = S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + cytidine 5'-{[hydroxy(2-hydroxypropyl)phosphonoyl]phosphate} + oxidized acceptor

For diagram of reaction, click here

Other name(s): Fom3; S-adenosyl-L-methionine:methylcob(III)alamin:2-hydroxyethylphosphonate methyltransferase (incorrect); 2-hydroxyethylphosphonate methyltransferase (incorrect)

Systematic name: S-adenosyl-L-methionine:cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} C-methyltransferase

Comments: Requires cobalamin. The enzyme, isolated from the bacterium Streptomyces wedmorensis, is involved in fosfomycin biosynthesis. It is a radical S-adenosyl-L-methionine (SAM) enzyme that contains a [4Fe-4S] center and a methylcob(III)alamin cofactor. The enzyme uses two molecues of SAM for the reaction. One molecule forms a 5'-deoxyadenosyl radical, while the other is used to methylate the cobalamin cofactor. The 5'-deoxyadenosyl radical abstracts a hydrogen from the C2 position of cytidine 5'-{[(2-hydroxyethyl)phosphonoyl]phosphate} forming a free radical that reacts with the methyl group on methylcob(III)alamin at the opposite side from SAM and the [4Fe-4S]cluster to produce a racemic mix of methylated products and cob(II)alamin. Both the [4Fe-4S]cluster and the cob(II)alamin need to be reduced by an unknown factor(s) before the enzyme could catalyse another cycle.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc

References:

1. Woodyer, R.D., Li, G., Zhao, H. and van der Donk, W.A. New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin. Chem. Commun. (Camb.) (2007) 359-361. [PMID: 17220970]

2. Allen, K.D. and Wang, S.C. Initial characterization of Fom3 from Streptomyces wedmorensis: The methyltransferase in fosfomycin biosynthesis. Arch. Biochem. Biophys. 543 (2014) 67-73. [PMID: 24370735]

3. Sato, S., Kudo, F., Kim, S.Y., Kuzuyama, T. and Eguchi, T. Methylcobalamin-dependent radical SAM C-methyltransferase Fom3 recognizes cytidylyl-2-hydroxyethylphosphonate and catalyzes the nonstereoselective C-methylation in fosfomycin biosynthesis. Biochemistry 56 (2017) 3519-3522. [PMID: 28678474]

4. Blaszczyk, A.J. and Booker, S.J. A (re)discovery of the Fom3 substrate. Biochemistry 57 (2018) 891-892. [PMID: 29345912]

[EC 2.1.1.308 created 2014, modified 2019]

EC 2.1.1.309

Accepted name: 18S rRNA (guanine1575-N7)-methyltransferase

Reaction: S-adenosyl-L-methionine + guanine1575 in 18S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine1575 in 18S rRNA

Other name(s): 18S rRNA methylase Bud23; BUD23 (gene name)

Systematic name: S-adenosyl-L-methionine:18S rRNA (guanine1575-N7)-methyltransferase

Comments: The enzyme, found in eukaryotes, is involved in pre-rRNA processing. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].

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

References:

1. White, J., Li, Z., Sardana, R., Bujnicki, J.M., Marcotte, E.M. and Johnson, A.W. Bud23 methylates G1575 of 18S rRNA and is required for efficient nuclear export of pre-40S subunits. Mol. Cell Biol. 28 (2008) 3151-3161. [PMID: 18332120]

[EC 2.1.1.309 created 2014]

EC 2.1.1.310

Accepted name: 25S rRNA (cytosine2870-C5)-methyltransferase

Reaction: S-adenosyl-L-methionine + cytosine2870 in 25S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA

Other name(s): NOP2 (gene name)

Systematic name: S-adenosyl-L-methionine:25S rRNA (cytosine2870-C5)-methyltransferase

Comments: The enzyme, found in eukaryotes, is specific for cytosine2870 of the 25S ribosomal RNA. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].

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

References:

1. Sharma, S., Yang, J., Watzinger, P., Kotter, P. and Entian, K.D. Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively. Nucleic Acids Res. 41 (2013) 9062-9076. [PMID: 23913415]

[EC 2.1.1.310 created 2014]

EC 2.1.1.311

Accepted name: 25S rRNA (cytosine2278-C5)-methyltransferase

Reaction: S-adenosyl-L-methionine + cytosine2278 in 25S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine2278 in 25S rRNA

Other name(s): RCM1 (gene name)

Systematic name: S-adenosyl-L-methionine:25S rRNA (cytosine2278-C5)-methyltransferase

Comments: The enzyme, found in eukaryotes, is specific for 25S cytosine2278. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].

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

References:

1. Sharma, S., Yang, J., Watzinger, P., Kotter, P. and Entian, K.D. Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively. Nucleic Acids Res. 41 (2013) 9062-9076. [PMID: 23913415]

[EC 2.1.1.311 created 2014]

EC 2.1.1.312

Accepted name: 25S rRNA (uracil2843-N3)-methyltransferase

Reaction: S-adenosyl-L-methionine + uracil2843 in 25S rRNA = S-adenosyl-L-homocysteine + N3-methyluracil2843 in 25S rRNA

Other name(s): BMT6

Systematic name: S-adenosyl-L-methionine:tRNA (uracil2843-N3)-methyltransferase

Comments: The enzyme, described from the yeast Saccharomyces cerevisiae, is involved in ribosome biogenesis.

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

References:

1. Sharma, S., Yang, J., Duttmann, S., Watzinger, P., Kotter, P. and Entian, K.D. Identification of novel methyltransferases, Bmt5 and Bmt6, responsible for the m3U methylations of 25S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res. 42 (2014) 3246-3260. [PMID: 24335083]

[EC 2.1.1.312 created 2014]

EC 2.1.1.313

Accepted name: 25S rRNA (uracil2634-N3)-methyltransferase

Reaction: S-adenosyl-L-methionine + uracil2634 in 25S rRNA = S-adenosyl-L-homocysteine + N3-methyluracil2634 in 25S rRNA

Other name(s): BMT5

Systematic name: S-adenosyl-L-methionine:tRNA (uracil2634-N3)-methyltransferase

Comments: The enzyme, described from the yeast Saccharomyces cerevisiae, is involved in ribosome biogenesis.

References:

1. Sharma, S., Yang, J., Duttmann, S., Watzinger, P., Kotter, P. and Entian, K.D. Identification of novel methyltransferases, Bmt5 and Bmt6, responsible for the m3U methylations of 25S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res. 42 (2014) 3246-3260. [PMID: 24335083]

[EC 2.1.1.313 created 2014]

EC 2.1.1.314

Accepted name: diphthine methyl ester synthase

Reaction: 4 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] = 4 S-adenosyl-L-homocysteine + diphthine methyl ester-[translation elongation factor 2]

For diagram of reaction click here.

Glossary: diphthine methyl ester = 2-[(3S)-4-methoxy-4-oxo-3-(trimethylammonio)butyl]-L-histidine

Other name(s): S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous)

Systematic name: S-adenosyl-L-methionine:2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] methyltransferase (diphthine methyl ester-[translation elongation factor 2]-forming)

Comments: This eukaryotic enzyme is part of the biosynthetic pathway of diphthamide. Different from the archaeal enzyme, which performs only 3 methylations, producing diphthine (cf. EC 2.1.1.98). The relevant histidine of elongation factor 2 is His715 in mammals and His699 in yeast. The order of the 4 methylations is not known.

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

References:

1. Chen, J.-Y.C. and Bodley, J.W. Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine:elongation factor 2 methyltransferase. J. Biol. Chem. 263 (1988) 11692-11696. [PMID: 3042777]

2. Moehring, J.M. and Moehring, T.J. The post-translational trimethylation of diphthamide studied in vitro. J. Biol. Chem. 263 (1988) 3840-3844. [PMID: 3346227]

3. Lin, Z., Su, X., Chen, W., Ci, B., Zhang, S. and Lin, H. Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis. J. Am. Chem. Soc. 136 (2014) 6179-6182. [PMID: 24739148]

[EC 2.1.1.314 created 2015]

EC 2.1.1.315

Accepted name: 27-O-demethylrifamycin SV methyltransferase

Reaction: S-adenosyl-L-methionine + 27-O-demethylrifamycin SV = S-adenosyl-L-homocysteine + rifamycin SV

Glossary: rifamycin SV = (7S,9E,11S,12R,13S,14R,15R,16R,17S,18S,19E,21Z)-2,15,17,27,29-pentahydroxy-11-methoxy-3,7,12,14,16,18,22-heptamethyl-6,23-dioxo-8,30-dioxa-24-azatetracyclo[23.3.1.14,7.05,28]triaconta-1(28),2,4,9, 19,21,25(29),26-octaen-13-yl acetate

Other name(s): AdoMet:27-O-demethylrifamycin SV methyltransferase

Systematic name: S-adenosyl-L-methionine:27-O-demethylrifamycin-SV 27-O-methyltransferase

Comments: The enzyme, characterized from the bacterium Amycolatopsis mediterranei, is involved in biosynthesis of the antitubercular drug rifamycin B.

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

References:

1. Xu, J., Mahmud, T. and Floss, H.G. Isolation and characterization of 27-O-demethylrifamycin SV methyltransferase provides new insights into the post-PKS modification steps during the biosynthesis of the antitubercular drug rifamycin B by Amycolatopsis mediterranei S699. Arch. Biochem. Biophys. 411 (2003) 277-288. [PMID: 12623077]

[EC 2.1.1.315 created 2015]

EC 2.1.1.316

Accepted name: mitomycin 6-O-methyltransferase

Reaction: (1) S-adenosyl-L-methionine + 6-demethylmitomycin A = S-adenosyl-L-homocysteine + mitomycin A
(2) S-adenosyl-L-methionine + 6-demethylmitomycin B = S-adenosyl-L-homocysteine + mitomycin B

Glossary: mitomycin A = [(1aS,8S,8aR,8bS)-5-methyl-6,8a-dimethoxy-4,7-dioxo-1,1a,2,4,7,8,8a,8b-octahydroazirino[2',3':3,4]pyrrolo[1,2-a]indol-8-yl]methyl carbamate
mitomycin B = [(1aS,8S,8aR,8bS)-8a-hydroxy-5-methyl-6-methoxy-4,7-dioxo-1,1a,2,4,7,8,8a,8b-octahydroazirino[2',3':3,4]pyrrolo[1,2-a]indol-8-yl]methyl carbamate

Other name(s): MmcR; mitomycin 7-O-methyltransferase (incorrect); S-adenosyl-L-methionine:7-demethylmitomycin-A 7-O-methyltransferase (incorrect)

Systematic name: S-adenosyl-L-methionine:6-demethylmitomycin-A 6-O-methyltransferase

Comments: The enzyme, characterized from the bacterium Streptomyces lavendulae, is involved in the biosynthesis of the quinone-containing antibiotics mitomycin A and mitomycin B.

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

References:

1. Gruschow, S., Chang, L.C., Mao, Y. and Sherman, D.H. Hydroxyquinone O-methylation in mitomycin biosynthesis. J. Am. Chem. Soc. 129 (2007) 6470-6476. [PMID: 17461583]

2. Singh, S., Chang, A., Goff, R.D., Bingman, C.A., Gruschow, S., Sherman, D.H., Phillips, G.N., Jr. and Thorson, J.S. Structural characterization of the mitomycin 7-O-methyltransferase. Proteins 79 (2011) 2181-2188. [PMID: 21538548]

[EC 2.1.1.316 created 2015]

EC 2.1.1.317

Accepted name: sphingolipid C9-methyltransferase

Reaction: S-adenosyl-L-methionine + a (4E,8E)-sphinga-4,8-dienine ceramide = S-adenosyl-L-homocysteine + a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide

Systematic name: S-adenosyl-L-methionine:(4E,8E)-sphinga-4,8-dienine ceramide C-methyltransferase

Comments: The enzyme, characterized from the fungi Komagataella pastoris and Fusarium graminearum, acts only on ceramides and has no activity with free sphingoid bases or glucosylceramides.

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

References:

1. Ternes, P., Sperling, P., Albrecht, S., Franke, S., Cregg, J.M., Warnecke, D. and Heinz, E. Identification of fungal sphingolipid C9-methyltransferases by phylogenetic profiling. J. Biol. Chem. 281 (2006) 5582-5592. [PMID: 16339149]

2. Ramamoorthy, V., Cahoon, E.B., Thokala, M., Kaur, J., Li, J. and Shah, D.M. Sphingolipid C-9 methyltransferases are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum. Eukaryot Cell 8 (2009) 217-229. [PMID: 19028992]

[EC 2.1.1.317 created 2015]

EC 2.1.1.318

Accepted name: [trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase

Reaction: S-adenosyl-L-methionine + [trehalose-6-phosphate synthase]-L-cysteine = S-adenosyl-L-homocysteine + [trehalose-6-phosphate synthase]-S-methyl-L-cysteine

Systematic name: S-adenosyl-L-methionine:[trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase

Comments: The enzyme, characterized from the yeast Saccharomyces cerevisiae, enhances the activity of EC 2.4.1.15, trehalose-6-phosphate synthase, resulting in elevating the levels of trehalose in the cell and contributing to stationary phase survival. In vitro the enzyme performs S-methylation of L-cysteine residues of various protein substrates.

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

References:

1. Sengupta, S., Banerjee, S., Lahiri, S., Dutta, T., Dhar, T.K. and Ghosh, A.K. Purification, characterization, sequencing and molecular cloning of a novel cysteine methyltransferase that regulates trehalose-6-phosphate synthase from Saccharomyces cerevisiae. Biochim. Biophys. Acta 1840 (2014) 1861-1871. [PMID: 24412193]

[EC 2.1.1.318 created 2015]

EC 2.1.1.319

Accepted name: type I protein arginine methyltransferase

Reaction: 2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-Nω,Nω-dimethyl-L-arginine (overall reaction)
(1a) S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω-methyl-L-arginine
(1b) S-adenosyl-L-methionine + [protein]-Nω-methyl-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω,Nω-dimethyl-L-arginine

Other name(s): PRMT1 (gene name); PRMT2 (gene name); PRMT3 (gene name); PRMT4 (gene name); PRMT6 (gene name); PRMT8 (gene name); RMT1 (gene name); CARM1 (gene name)

Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nω,Nω-dimethyl-L-arginine-forming)

Comments: This eukaryotic enzyme catalyses the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues [1]. PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells [2]. cf. EC 2.1.1.320, type II protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.

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

References:

1. Gary, J.D. and Clarke, S. RNA and protein interactions modulated by protein arginine methylation. Prog. Nucleic Acid Res. Mol. Biol. 61 (1998) 65-131. [PMID: 9752719]

2. Tang, J., Gary, J.D., Clarke, S. and Herschman, H.R. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J. Biol. Chem. 273 (1998) 16935-16945. [PMID: 9642256]

3. Tang, J., Frankel, A., Cook, R.J., Kim, S., Paik, W.K., Williams, K.R., Clarke, S. and Herschman, H.R. PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells. J. Biol. Chem. 275 (2000) 7723-7730. [PMID: 10713084]

4. Frankel, A., Yadav, N., Lee, J., Branscombe, T.L., Clarke, S. and Bedford, M.T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277 (2002) 3537-3543. [PMID: 11724789]

[EC 2.1.1.319 created 2015]

EC 2.1.1.320

Accepted name: type II protein arginine methyltransferase

Reaction: 2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-Nω,Nω'-dimethyl-L-arginine (overall reaction)
(1a) S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω-methyl-L-arginine
(1b) S-adenosyl-L-methionine + [protein]-Nω-methyl-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω,Nω'-dimethyl-L-arginine

Other name(s): PRMT5 (gene name); PRMT9 (gene name)

Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nω,Nω'-dimethyl-L-arginine-forming)

Comments: The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.

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

References:

1. Branscombe, T.L., Frankel, A., Lee, J.H., Cook, J.R., Yang, Z., Pestka, S. and Clarke, S. PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. J. Biol. Chem. 276 (2001) 32971-32976. [PMID: 11413150]

2. Wang, X., Zhang, Y., Ma, Q., Zhang, Z., Xue, Y., Bao, S. and Chong, K. SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis. EMBO J. 26 (2007) 1934-1941. [PMID: 17363895]

3. Lacroix, M., El Messaoudi, S., Rodier, G., Le Cam, A., Sardet, C. and Fabbrizio, E. The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5. EMBO Rep. 9 (2008) 452-458. [PMID: 18404153]

4. Chari, A., Golas, M.M., Klingenhager, M., Neuenkirchen, N., Sander, B., Englbrecht, C., Sickmann, A., Stark, H. and Fischer, U. An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs. Cell 135 (2008) 497-509. [PMID: 18984161]

5. Antonysamy, S., Bonday, Z., Campbell, R.M., Doyle, B., Druzina, Z., Gheyi, T., Han, B., Jungheim, L.N., Qian, Y., Rauch, C., Russell, M., Sauder, J.M., Wasserman, S.R., Weichert, K., Willard, F.S., Zhang, A. and Emtage, S. Crystal structure of the human PRMT5:MEP50 complex. Proc. Natl. Acad. Sci. USA 109 (2012) 17960-17965. [PMID: 23071334]

6. Hadjikyriacou, A., Yang, Y., Espejo, A., Bedford, M.T. and Clarke, S.G. Unique features of human protein arginine methyltransferase 9 (PRMT9) and its substrate RNA splicing factor SF3B2. J. Biol. Chem. 290 (2015) 16723-16743. [PMID: 25979344]

[EC 2.1.1.320 created 2015]

EC 2.1.1.321

Accepted name: type III protein arginine methyltransferase

Reaction: S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nω-methyl-L-arginine

Other name(s): PRMT7 (gene name)

Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nω-methyl-L-arginine-forming)

Comments: Type III protein arginine methyltransferases catalyse the single methylation of one of the terminal nitrogen atoms of the guanidino group in an L-arginine residue within a protein. Unlike type I and type II protein arginine methyltransferases, which also catalyse this reaction, type III enzymes do not methylate the substrate any further. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.320, type II protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.

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

References:

1. Miranda, T.B., Miranda, M., Frankel, A. and Clarke, S. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J. Biol. Chem. 279 (2004) 22902-22907. [PMID: 15044439]

2. Gonsalvez, G.B., Tian, L., Ospina, J.K., Boisvert, F.M., Lamond, A.I. and Matera, A.G. Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J. Cell Biol. 178 (2007) 733-740. [PMID: 17709427]

3. Feng, Y., Hadjikyriacou, A. and Clarke, S.G. Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop. J. Biol. Chem. 289 (2014) 32604-32616. [PMID: 25294873]

[EC 2.1.1.321 created 2015]

EC 2.1.1.322

Accepted name: type IV protein arginine methyltransferase

Reaction: S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N5-methyl-L-arginine

Other name(s): RMT2 (gene name)

Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-N5-methyl-L-arginine-forming)

Comments: This enzyme, characterized from the yeast Saccharomyces cerevisiae, methylates the the δ-nitrogen atom of arginine residues within proteins. Among its substrates are Arg67 of the ribosomal protein L12. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.320, type II protein arginine methyltransferase, and EC 2.1.1.321, type III protein arginine methyltransferase.

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

References:

1. Niewmierzycka, A. and Clarke, S. S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. J. Biol. Chem. 274 (1999) 814-824. [PMID: 9873020]

2. Chern, M.K., Chang, K.N., Liu, L.F., Tam, T.C., Liu, Y.C., Liang, Y.L. and Tam, M.F. Yeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2. J. Biol. Chem. 277 (2002) 15345-15353. [PMID: 11856739]

3. Olsson, I., Berrez, J.M., Leipus, A., Ostlund, C. and Mutvei, A. The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100. Exp Cell Res 313 (2007) 1778-1789. [PMID: 17448464]

[EC 2.1.1.322 created 2015]

EC 2.1.1.323

Accepted name:(–)-pluviatolide 4-O-methyltransferase

Reaction: S-adenosyl-L-methionine + (–)-pluviatolide = S-adenosyl-L-homocysteine + (–)-bursehernin

For diagram of reaction click here.

Glossary:(–)-pluviatolide = (3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(4-hydroxy-3-methoxyphenyl)methyl]oxolan-2-one
(–)-bursehernin = (3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(3,4-dimethoxyphenyl)methyl]oxolan-2-one

Other name(s): OMT3 (gene name)

Systematic name: S-adenosyl-L-methionine:(–)-pluviatolide 4-O-methyltransferase

Comments: The enzyme, characterized from the plant Sinopodophyllum hexandrum, is involved in the biosynthetic pathway of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs.

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

References:

1. Lau, W. and Sattely, E.S. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone. Science 349 (2015) 1224-1228. [PMID: 26359402]

[EC 2.1.1.323 created 2016]

EC 2.1.1.324

Accepted name: dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase

Reaction: 2 S-adenosyl-L-methionine + dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose = 2 S-adenosyl-L-homocysteine + dTDP-α-D-forosamine (overall reaction)
(1a) S-adenosyl-L-methionine + dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose = S-adenosyl-L-homocysteine + dTDP-4-(methylamino)-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose
(1b) 2 S-adenosyl-L-methionine + dTDP-4-(methylamino)-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose = 2 S-adenosyl-L-homocysteine + dTDP-α-D-forosamine

For diagram of reaction click here.

Glossary: dTDP-α-D-forosamine = dTDP-4-(dimethylamino)-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose

Other name(s): SpnS; TDP-4-amino-2,3,6-trideoxy-D-glucose N,N-dimethyltransferase

Systematic name: S-adenosyl-L-methionine:dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose N,N-dimethyltransferase

Comments: The enzyme was isolated from the bacterium Saccharopolyspora spinosa, where it is involved in the biosynthesis of spinosyn A, an active ingredient of several commercial insecticides.

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

References:

1. Hong, L., Zhao, Z., Melancon, C.E., 3rd, Zhang, H. and Liu, H.W. In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa, J. Am. Chem. Soc. 130 (2008) 4954-4967. [PMID: 18345667]

[EC 2.1.1.324 created 2016]

EC 2.1.1.325

Accepted name: juvenile hormone-III synthase

Reaction: (1) S-adenosyl-L-methionine + (2E,6E)-farnesoate = S-adenosyl-L-homocysteine + methyl (2E,6E)-farnesoate
(2) S-adenosyl-L-methionine + juvenile hormone III acid = S-adenosyl-L-homocysteine + juvenile hormone III

Glossary: juvenile hormone III = methyl (2E,6E,10R)-10,11-epoxy-3,7,11-trimethyldodeca-2,6-dienoate
juvenile hormone III acid = (2E,6E,10R)-10,11-epoxy-3,7,11-trimethyldodeca-2,6-dienoate

Other name(s): farnesoic acid methyltransferase; juvenile hormone acid methyltransferase; JHAMT

Systematic name: S-adenosyl-L-methionine:(2E,6E)-farnesoate O-methyltransferase

Comments: The enzyme, found in insects, is involved in the synthesis of juvenile hormone III, a sesquiterpenoid that regulates several processes including embryonic development, metamorphosis, and reproduction, in many insect species.

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

References:

1. Shinoda, T. and Itoyama, K. Juvenile hormone acid methyltransferase: a key regulatory enzyme for insect metamorphosis. Proc. Natl. Acad. Sci. USA 100 (2003) 11986-11991. [PMID: 14530389]

2. Defelipe, L.A., Dolghih, E., Roitberg, A.E., Nouzova, M., Mayoral, J.G., Noriega, F.G. and Turjanski, A.G. Juvenile hormone synthesis: "esterify then epoxidize" or "epoxidize then esterify"? Insights from the structural characterization of juvenile hormone acid methyltransferase. Insect Biochem. Mol. Biol. 41 (2011) 228-235. [PMID: 21195763]

3. Van Ekert, E., Heylen, K., Rouge, P., Powell, C.A., Shatters, R.G., Jr., Smagghe, G. and Borovsky, D. Aedes aegypti juvenile hormone acid methyl transferase, the ultimate enzyme in the biosynthetic pathway of juvenile hormone III, exhibits substrate control. J. Insect Physiol. 64 (2014) 62-73. [PMID: 24657668]

4. Van Ekert, E., Shatters, R.G., Jr., Rouge, P., Powell, C.A., Smagghe, G. and Borovsky, D. Cloning and expressing a highly functional and substrate specific farnesoic acid o-methyltransferase from the Asian citrus psyllid (Diaphorina citri Kuwayama). FEBS Open Bio 5 (2015) 264-275. [PMID: 25893162]

[EC 2.1.1.325 created 2016]

EC 2.1.1.326

Accepted name: N-acetyl-demethylphosphinothricin P-methyltransferase

Reaction: 2 S-adenosyl-L-methionine + N-acetyl-demethylphosphinothricin + reduced acceptor = S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + N-acetyl-phosphinothricin + oxidized acceptor

Glossary: N-acetyl-demethylphosphinothricin = (2S)-2-acetamido-4-phosphinatobutanoate

Other name(s): phpK (gene name); bcpD (gene name); P-methylase

Systematic name: S-adenosyl-L-methionine:N-acetyl-demethylphosphinothricin P-methyltransferase

Comments: The enzyme was originally characterized from bacteria that produce the tripeptides bialaphos and phosalacine, which inhibit plant and bacterial glutamine synthetases. It is a radical S-adenosyl-L-methionine (SAM) enzyme that contains a [4Fe-4S] center and a methylcob(III)alamin cofactor. According to the proposed mechanism, the reduced iron-sulfur center donates an electron to SAM, resulting in homolytic cleavage of the carbon-sulfur bond to form a 5'-deoxyadenosyl radical that abstracts the hydrogen atom from the P-H bond of the substrate, forming a phosphinate-centered radical. This radical reacts with methylcob(III)alamin to produce the methylated product and cob(II)alamin, which is reduced by an unknown donor to cob(I)alamin. A potential route for restoring the latter back to methylcob(III)alamin is a nucleophilic attack on a second SAM molecule. The enzyme acts in vivo on N-acetyl-demethylphosphinothricin-L-alanyl-L-alanine or N-acetyl-demethylphosphinothricin-L-alanyl-L-leucine, the intermediates in the biosynthesis of bialaphos and phosalacine, respectively. This transformation produces the only example of a carbon-phosphorus-carbon linkage known to occur in nature.

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

References:

1. Kamigiri, K., Hidaka, T., Imai, S., Murakami, T. and Seto, H. Studies on the biosynthesis of bialaphos (SF-1293) 12. C-P bond formation mechanism of bialaphos: discovery of a P-methylation enzyme. J. Antibiot. (Tokyo) 45 (1992) 781-787. [PMID: 1624380]

2. Hidaka, T., Hidaka, M., Kuzuyama, T. and Seto, H. Sequence of a P-methyltransferase-encoding gene isolated from a bialaphos-producing Streptomyces hygroscopicus. Gene 158 (1995) 149-150. [PMID: 7789803]

3. Werner, W.J., Allen, K.D., Hu, K., Helms, G.L., Chen, B.S. and Wang, S.C. In vitro phosphinate methylation by PhpK from Kitasatospora phosalacinea. Biochemistry 50 (2011) 8986-8988. [PMID: 21950770]

4. Allen, K.D. and Wang, S.C. Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217. Biochim. Biophys. Acta 1844 (2014) 2135-2144. [PMID: 25224746]

5. Hu, K., Werner, W.J., Allen, K.D. and Wang, S.C. Investigation of enzymatic C-P bond formation using multiple quantum HCP nuclear magnetic resonance spectroscopy. Magn. Reson. Chem. 53 (2015) 267-272. [PMID: 25594737]

[EC 2.1.1.326 created 2016]

EC 2.1.1.327

Accepted name: phenazine-1-carboxylate N-methyltransferase

Reaction: S-adenosyl-L-methionine + phenazine-1-carboxylate = S-adenosyl-L-homocysteine + 5-methyl-phenazine-1-carboxylate

For diagram of reaction click here.

Other name(s): phzM (gene name)

Systematic name: S-adenosyl-L-methionine:phenazine-1-carboxylate 5-N-methyltransferase

Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in the biosynthesis of pyocyanin, a toxin produced and secreted by the organism. The enzyme is active in vitro only in the presence of EC 1.14.13.218, 5-methylphenazine-1-carboxylate 1-monooxygenase.

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

References:

1. Parsons, J.F., Greenhagen, B.T., Shi, K., Calabrese, K., Robinson, H. and Ladner, J.E. Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa. Biochemistry 46 (2007) 1821-1828. [PMID: 17253782]

[EC 2.1.1.327 created 2016]

EC 2.1.1.328

Accepted name: N-demethylindolmycin N-methyltransferase

Reaction: S-adenosyl-L-methionine + N-demethylindolmycin = S-adenosyl-L-homocysteine + indolmycin

Glossary: indolmycin = (5S)-5-[(1R)-1-(indol-3-yl)ethyl]-2-(methylamino)-1,3-oxazolin-4(5H)-one

Other name(s): ind7 (gene name)

Systematic name: S-adenosyl-L-methionine:N-demethylindolmycin N-methyltransferase

Comments: The enzyme, characterized from the bacterium Streptomyces griseus, catalyses the ultimate reaction in the biosynthesis of indolmycin, an antibacterial drug that inhibits the bacterial tryptophan—tRNA ligase (EC 6.1.1.2).

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

References:

1. Du, Y.L., Alkhalaf, L.M. and Ryan, K.S. In vitro reconstitution of indolmycin biosynthesis reveals the molecular basis of oxazolinone assembly. Proc. Natl. Acad. Sci. USA 112 (2015) 2717-2722. [PMID: 25730866]

[EC 2.1.1.328 created 2016]

EC 2.1.1.329

Accepted name: demethylphylloquinol methyltransferase

Reaction: S-adenosyl-L-methionine + demethylphylloquinol = S-adenosyl-L-homocysteine + phylloquinol

For diagram of reaction click here.

Glossary: demethylphylloquinol = 2-phytyl-1,4-naphthoquinol
phylloquinol = 2-methyl-3-phytyl-1,4-naphthoquinol = vitamin K1

Other name(s): menG (gene name); 2-phytyl-1,4-naphthoquinol methyltransferase

Systematic name: S-adenosyl-L-methionine:2-phytyl-1,4-naphthoquinol C-methyltransferase

Comments: The enzyme, found in plants and cyanobacteria, catalyses the final step in the biosynthesis of phylloquinone (vitamin K1), an electron carrier associated with photosystem I. The enzyme is specific for the quinol form of the substrate, and does not act on the quinone form [3].

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

References:

1. Sakuragi, Y., Zybailov, B., Shen, G., Jones, A.D., Chitnis, P.R., van der Est, A., Bittl, R., Zech, S., Stehlik, D., Golbeck, J.H. and Bryant, D.A. Insertional inactivation of the menG gene, encoding 2-phytyl-1,4-naphthoquinone methyltransferase of Synechocystis sp. PCC 6803, results in the incorporation of 2-phytyl-1,4-naphthoquinone into the A1 site and alteration of the equilibrium constant between A1 and F(X) in photosystem I. Biochemistry 41 (2002) 394-405. [PMID: 11772039]

2. Lohmann, A., Schottler, M.A., Brehelin, C., Kessler, F., Bock, R., Cahoon, E.B. and Dormann, P. Deficiency in phylloquinone (vitamin K1) methylation affects prenyl quinone distribution, photosystem I abundance, and anthocyanin accumulation in the Arabidopsis AtmenG mutant. J. Biol. Chem. 281 (2006) 40461-40472. [PMID: 17082184]

3. Fatihi, A., Latimer, S., Schmollinger, S., Block, A., Dussault, P.H., Vermaas, W.F., Merchant, S.S. and Basset, G.J. A dedicated type II NADPH dehydrogenase performs the penultimate step in the biosynthesis of vitamin K1 in Synechocystis and Arabidopsis. Plant Cell 27 (2015) 1730-1741. [PMID: 26023160]

[EC 2.1.1.329 created 2016]

EC 2.1.1.330

Accepted name: 5'-demethylyatein 5'-O-methyltransferase

Reaction: S-adenosyl-L-methionine + (–)-5'-demethylyatein = S-adenosyl-L-homocysteine + (-)-yatein

For diagram of reaction click here.

Glossary: (–)-5'-demethylyatein = (3R,4R)-4-(2,3-benzodioxol-5-ylmethyl)-3-(3-hydroxy-4,5-dimethoxybenzyl)dihydrofuran-2(3H)-one
(–)-yatein = (3R,4R)-4-(1,3-benzodioxol-5-ylmethyl)-3-(3,4,5-trimethoxybenzyl)dihydrofuran-2(3H)-one

Other name(s): OMT1 (gene name)

Systematic name: S-adenosyl-L-methionine:(–)-5'-demethylyatein 5'-O-methyltransferase

Comments: The enzyme, characterized from the plant Sinopodophyllum hexandrum, is involved in the biosynthetic pathway of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs.

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

References:

1. Lau, W. and Sattely, E.S. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone. Science 349 (2015) 1224-1228. [PMID: 26359402]

[EC 2.1.1.330 created 2016]

EC 2.1.1.331

Accepted name: bacteriochlorophyllide d C-121-methyltransferase

Reaction: S-adenosyl-L-methionine + 8-ethyl-12-methyl-3-vinylbacteriochlorophyllide d = S-adenosyl-L-homocysteine + 8,12-diethyl-3-vinylbacteriochlorophyllide d

For diagram of reaction click here.

Other name(s): bchR (gene name)

Systematic name: S-adenosyl-L-methionine:8-ethyl-12-methyl-3-vinylbacteriochlorophyllide-d C-121-methyltransferase

Comments: This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is a radical S-adenosyl-L-methionine (AdoMet) enzyme and contains a [4Fe-4S] cluster. It adds a methyl group at the C-121 position of bacteriochlorophylls of the c, d and e types. This methylation plays a role in fine-tuning the structural arrangement of the bacteriochlorophyll aggregates in chlorosomes and therefore directly influences the chlorosomes absorption properties.

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

References:

1. Gomez Maqueo Chew, A., Frigaard, N.U. and Bryant, D.A. Bacteriochlorophyllide c C-82 and C-121 methyltransferases are essential for adaptation to low light in Chlorobaculum tepidum. J. Bacteriol. 189 (2007) 6176-6184. [PMID: 17586634]

[EC 2.1.1.331 created 2016]

EC 2.1.1.332

Accepted name: bacteriochlorophyllide d C-82-methyltransferase

Reaction: (1) S-adenosyl-L-methionine + 8,12-diethyl-3-vinylbacteriochlorophyllide d = S-adenosyl-L-homocysteine + 12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d
(2) S-adenosyl-L-methionine + 12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d = S-adenosyl-L-homocysteine + 12-ethyl-8-isobutyl-3-vinylbacteriochlorophyllide d

For diagram of reaction click here.

Other name(s): bchQ (gene name)

Systematic name: S-adenosyl-L-methionine:8,12-diethyl-3-vinylbacteriochlorophyllide-d C-82-methyltransferase

Comments: This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is a radical S-adenosyl-L-methionine (AdoMet) enzyme and contains a [4Fe-4S] cluster. It adds one or two methyl groups at the C-82 position of bacteriochlorophylls of the c, d and e types. These methylations play a role in fine-tuning the structural arrangement of the bacteriochlorophyll aggregates in chlorosomes and therefore directly influence chlorosomal absorption properties.

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

References:

1. Gomez Maqueo Chew, A., Frigaard, N.U. and Bryant, D.A. Bacteriochlorophyllide c C-82 and C-121 methyltransferases are essential for adaptation to low light in Chlorobaculum tepidum. J. Bacteriol. 189 (2007) 6176-6184. [PMID: 17586634]

[EC 2.1.1.332 created 2016]

EC 2.1.1.333

Accepted name: bacteriochlorophyllide d C-20 methyltransferase

Reaction: S-adenosyl-L-methionine + a bacteriochlorophyllide d = S-adenosyl-L-homocysteine + a bacteriochlorophyllide c

For diagram of reaction click here.

Other name(s): bchU (gene name)

Systematic name: S-adenosyl-L-methionine:bacteriochlorophyllide-d C-20 methyltransferase

Comments: The enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), catalyses the methylation of the C-20 methine bridge position in bacteriochlorophyllide d, forming bacteriochlorophyllide c.

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

References:

1. Maresca, J.A., Gomez Maqueo Chew, A., Ponsati, M.R., Frigaard, N.U., Ormerod, J.G. and Bryant, D.A. The bchU gene of Chlorobium tepidum encodes the c-20 methyltransferase in bacteriochlorophyll c biosynthesis. J. Bacteriol. 186 (2004) 2558-2566. [PMID: 15090495]

[EC 2.1.1.333 created 2016]

EC 2.1.1.334

Accepted name: methanethiol S-methyltransferase

Reaction: S-adenosyl-L-methionine + methanethiol = S-adenosyl-L-homocysteine + dimethyl sulfide

Other name(s): mddA (gene name)

Systematic name: S-adenosyl-L-methionine:methanethiol S-methyltransferase

Comments: The enzyme, found in many bacterial taxa, is involved in a pathway that converts L-methionine to dimethyl sulfide.

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

References:

1. Carrion, O., Curson, A.R., Kumaresan, D., Fu, Y., Lang, A.S., Mercade, E. and Todd, J.D. A novel pathway producing dimethylsulphide in bacteria is widespread in soil environments. Nat Commun 6 (2015) 6579. [PMID: 25807229]

[EC 2.1.1.334 created 2016]

EC 2.1.1.335

Accepted name: 4-amino-anhydrotetracycline N4-methyltransferase

Reaction: (1) S-adenosyl-L-methionine + 4-amino-4-de(dimethylamino)anhydrotetracycline = S-adenosyl-L-homocysteine + 4-methylamino-4-de(dimethylamino)anhydrotetracycline
(2) S-adenosyl-L-methionine + 4-methylamino-4-de(dimethylamino)anhydrotetracycline = S-adenosyl-L-homocysteine + anhydrotetracycline

For diagram of reaction click here.

Glossary: 4-amino-4-de(dimethylamino)anhydrotetracycline = (4S,4aS,12aS)-4-amino-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-4a,5-dihydro-4H-tetracene-2-carboxamide
4-methylamino-4-de(dimethylamino)anhydrotetracycline = (4S,4aS,12aS)-3,10,11,12a-tetrahydroxy-6-methyl-4-(methylamino)-1,12-dioxo-4a,5-dihydro-4H-tetracene-2-carboxamide
anhydrotetracycline = (4S,4aS,12aS)-4-(dimethylamino)-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-1,4,4a,5,12,12a-hexahydrotetracene-2-carboxamide

Other name(s): oxyT (gene name); ctcO (gene name)

Systematic name: S-adenosyl-L-methionine:(4S,4aS,12aS)-4-amino-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-4a,5-dihydro-4H-tetracene-2-carboxamide Nα-methyltransferase

Comments: The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics.

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

References:

1. Zhang, W., Watanabe, K., Cai, X., Jung, M.E., Tang, Y. and Zhan, J. Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. J. Am. Chem. Soc. 130 (2008) 6068-6069. [PMID: 18422316]

[EC 2.1.1.335 created 2016]

EC 2.1.1.336

Accepted name: norbelladine O-methyltransferase

Reaction: S-adenosyl-L-methionine + norbelladine = S-adenosyl-L-homocysteine + 4'-O-methylnorbelladine

For diagram of reaction click here.

Glossary: norbelladine = 4-({[2-(4-hydroxyphenyl)ethyl]amino}methyl)benzene-1,2-diol
4'-O-methylnorbelladine = 5-({[2-(4-hydroxyphenyl)ethyl]amino}methyl)-2-methoxyphenol

Other name(s): N4OMT1 (gene name)

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

Comments: The enzyme, characterized from the plants Nerine bowdenii and Narcissus pseudonarcissus (daffodil), participates in the biosynthesis of alkaloids produced by plants that belong to the Amaryllidaceae family.

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

References:

1. Mann, J.D., Fales, H.M. and Mudd, S.H. Alkaloids and plant metabolism. VI. O-methylation in vitro of norbelladine, a precursor of Amaryllidaceae alkaloids. J. Biol. Chem. 238 (1963) 3820-3823. [PMID: 14109227]

2. Kilgore, M.B., Augustin, M.M., Starks, C.M., O'Neil-Johnson, M., May, G.D., Crow, J.A. and Kutchan, T.M. Cloning and characterization of a norbelladine 4'-O-methyltransferase involved in the biosynthesis of the Alzheimer’s drug galanthamine in Narcissus sp. aff. pseudonarcissus. PLoS One 9 (2014) e103223. [PMID: 25061748]

[EC 2.1.1.336 created 2016]

EC 2.1.1.337

Accepted name: reticuline N-methyltransferase

Reaction: (1) S-adenosyl-L-methionine + (S)-reticuline = S-adenosyl-L-homocysteine + (S)-tembetarine
(2) S-adenosyl-L-methionine + (S)-corytuberine = S-adenosyl-L-homocysteine + magnoflorine

For diagram of reaction click here or click here

Glossary: (S)-reticuline = (1S)-1-(3-hydroxy-4-methoxybenzyl)-6-methoxy-2-methyl-1,2,3,4-tetrahydroisoquinolin-7-ol
(S)-tembetarine = (1S)-1-(3-hydroxy-4-methoxybenzyl)-6-methoxy-2,2-dimethyl-1,2,3,4-tetrahydroisoquinolin-7-ol
(S)-corytuberine = (6aS)-2,10-dimethoxy-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-1,11-diol
(S)-magnoflorine = (6aS)-1,11-dihydroxy-2,10-dimethoxy-6,6-dimethyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinolinium

Other name(s): RNMT

Systematic name: S-adenosyl-L-methionine:(S)-reticuline N-methyltransferase

Comments: The enzyme from opium poppy (Papaver somniferum) can also methylate (R)-reticuline, tetrahydropapaverine, (S)-glaucine and (S)-bulbocapnine. It is involved in the biosynthesis of the quaternary benzylisoquinoline alkaloid magnoflorine.

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

References:

1. Morris, J.S. and Facchini, P.J. Isolation and characterization of reticuline N-methyltransferase involved in biosynthesis of the aporphine alkaloid magnoflorine in opium poppy. J. Biol. Chem. 291 (2016) 23416-23427. [PMID: 27634038]

[EC 2.1.1.337 created 2017]

EC 2.1.1.338

Accepted name: desmethylxanthohumol 6'-O-methyltransferase

Reaction: S-adenosyl-L-methionine + desmethylxanthohumol = S-adenosyl-L-homocysteine + xanthohumol

For diagram of reaction click here.

Glossary: desmethylxanthohumol = (2E)-3-(4-hydroxyphenyl)-1-[2,4,6-trihydroxy-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-en-1-one
xanthohumol = (2E)-1-[2,4-dihydroxy-6-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-one

Other name(s): OMT1 (ambiguous)

Systematic name: S-adenosyl-L-methionine:desmethylxanthohumol 6'-O-methyltransferase

Comments: Found in hops (Humulus lupulus). The enzyme can also methylate xanthogalenol.

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

References:

1. Nagel, J., Culley, L.K., Lu, Y., Liu, E., Matthews, P.D., Stevens, J.F. and Page, J.E. EST analysis of hop glandular trichomes identifies an O-methyltransferase that catalyzes the biosynthesis of xanthohumol. Plant Cell 20 (2008) 186-200. [PMID: 18223037]

[EC 2.1.1.338 created 2017]

EC 2.1.1.339

Accepted name: xanthohumol 4-O-methyltransferase

Reaction: S-adenosyl-L-methionine + xanthohumol = S-adenosyl-L-homocysteine + 4-O-methylxanthohumol

For diagram of reaction click here

Glossary: xanthohumol = 2',4,4'-trihydroxy-6'-methoxy-3-prenylchalcone = (2E)-1-[2,4-dihydroxy-6-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-one
4-O-methylxanthohumol =2',4'-dihydroxy-4,6'-dimethoxy-3-prenylchalcone = (2E)-1-[2,4-dihydroxy-6-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]-3-(4-methoxyphenyl)prop-2-en-1-one

Other name(s): OMT2 (ambiguous); S-adenosyl-L-methionine:xanthohumol 4'-O-methyltransferase (incorrect); xanthohumol 4'-O-methyltransferase (incorrect)

Systematic name: S-adenosyl-L-methionine:xanthohumol 4-O-methyltransferase

Comments: The enzyme from hops (Humulus lupulus) has a broad substrate specificity. The best substrates in vitro are resveratrol, desmethylxanthohumol, naringenin chalcone and isoliquiritigenin.

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

References:

1. Nagel, J., Culley, L.K., Lu, Y., Liu, E., Matthews, P.D., Stevens, J.F. and Page, J.E. EST analysis of hop glandular trichomes identifies an O-methyltransferase that catalyzes the biosynthesis of xanthohumol. Plant Cell 20 (2008) 186-200. [PMID: 18223037]

[EC 2.1.1.339 created 2017, modified 2018]

EC 2.1.1.340

Accepted name: 3-aminomethylindole N-methyltransferase

Reaction: 2 S-adenosyl-L-methionine + 3-(aminomethyl)indole = 2 S-adenosyl-L-homocysteine + gramine (overall reaction)
(1a) S-adenosyl-L-methionine + 3-(aminomethyl)indole = S-adenosyl-L-homocysteine + (1H-indol-3-yl)-N-methylmethanamine
(1b) S-adenosyl-L-methionine + (1H-indol-3-yl)-N-methylmethanamine = S-adenosyl-L-homocysteine + gramine

For diagram of reaction click here.

Glossary: 3-(aminomethyl)indole = (1H-indol-3-yl)methanamine
gramine = (1H-indol-3-ylmethyl)dimethylamine = (1H-indol-3-yl)-N,N-dimethylmethanamine

Other name(s): NMT (gene name)

Systematic name: S-adenosyl-L-methionine:3-(aminomethyl)indole N-methyltransferase (gramine-forming)

Comments: The enzyme, characterized from Hordeum vulgare (barley), catalyses two successive N-methylation reactions during the biosynthesis of gramine, a toxic indole alkaloid.

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

References:

1. Leland, T.J. and Hanson, A.D. Induction of a specific N-methyltransferase enzyme by long-term heat stress during barley leaf growth. Plant Physiol. 79 (1985) 451-457. [PMID: 16664431]

2. Larsson, K.A., Zetterlund, I., Delp, G. and Jonsson, L.M. N-Methyltransferase involved in gramine biosynthesis in barley: cloning and characterization. Phytochemistry 67 (2006) 2002-2008. [PMID: 16930646]

[EC 2.1.1.340 created 2017]

EC 2.1.1.341

Accepted name: vanillate/3-O-methylgallate O-demethylase

Reaction: (1) vanillate + tetrahydrofolate = protocatechuate + 5-methyltetrahydrofolate
(2) 3-O-methylgallate + tetrahydrofolate = gallate + 5-methyltetrahydrofolate

Glossary: protocatechuate = 3,4-dihydroxybenzoate
vanillate = 4-hydroxy-3-methoxybenzoate
gallate = 3,4,5-trihydroxybenzoate

Other name(s): ligM (gene name)

Systematic name: vanillate:tetrahydrofolate O-methyltransferase

Comments: The enzyme, characterized from the bacterium Sphingomonas sp. SYK6, is involved in the degradation of lignin. The enzyme has similar activities with vanillate and 3-O-methylgallate.

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

References:

1. Nishikawa, S., Sonoki, T., Kasahara, T., Obi, T., Kubota, S., Kawai, S., Morohoshi, N. and Katayama, Y. Cloning and sequencing of the Sphingomonas (Pseudomonas) paucimobilis gene essential for the O demethylation of vanillate and syringate. Appl. Environ. Microbiol. 64 (1998) 836-842. [PMID: 9501423]

2. Masai, E., Sasaki, M., Minakawa, Y., Abe, T., Sonoki, T., Miyauchi, K., Katayama, Y. and Fukuda, M. A novel tetrahydrofolate-dependent O-demethylase gene is essential for growth of Sphingomonas paucimobilis SYK-6 with syringate. J. Bacteriol. 186 (2004) 2757-2765. [PMID: 15090517]

3. Abe, T., Masai, E., Miyauchi, K., Katayama, Y. and Fukuda, M. A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 187 (2005) 2030-2037. [PMID: 15743951]

[EC 2.1.1.341 created 2017]

EC 2.1.1.342

Accepted name: anaerobilin synthase

Reaction: 2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin

For diagram of reaction click here.

Glossary: anaerobilin = (4Z,10Z,14E)-8,12-bis(2-carboxyethyl)-3,7,13,18-tetramethyl-1,2,17-trivinyl-23,24-dihydrobilin

Other name(s): chuW (gene name)

Systematic name: S-adenosyl-L-methionine:protoheme C-methyltransferase (anaerobilin-producing)

Comments: The enzyme, studied from the bacterium Escherichia coli O157:H7, is a radical SAM (AdoMet) enzyme that is involved in heme degradation and iron utilization under anaerobic conditions. The enzyme uses two SAM molecules for the reaction. The first molecule is used to generate a 5'-deoxyadenosyl radical, which abstracts a hydrogen atom from the methyl group of the second SAM molecule. The newly formed methylene radical attacks the substrate, causing a rearrangement of the porphyrin ring that results in the liberation of iron.

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

References:

1. LaMattina, J.W., Nix, D.B. and Lanzilotta, W.N. Radical new paradigm for heme degradation in Escherichia coli O157:H7. Proc. Natl. Acad. Sci. USA 113 (2016) 12138-12143. [PMID: 27791000]

2. LaMattina, J.W., Delrossi, M., Uy, K.G., Keul, N.D., Nix, D.B., Neelam, A.R. and Lanzilotta, W.N. Anaerobic heme degradation: ChuY Is an anaerobilin reductase that exhibits kinetic cooperativity. Biochemistry 56 (2017) 845-855. [PMID: 28045510]

[EC 2.1.1.342 created 2017]

EC 2.1.1.343

Accepted name: 8-amino-8-demethylriboflavin N,N-dimethyltransferase

Reaction: 2 S-adenosyl-L-methionine + 8-amino-8-demethylriboflavin = 2 S-adenosyl-L-homocysteine + roseoflavin (overall reaction)
(1a) S-adenosyl-L-methionine + 8-amino-8-demethylriboflavin = S-adenosyl-L-homocysteine + 8-demethyl-8-(methylamino)riboflavin
(1b) S-adenosyl-L-methionine + 8-demethyl-8-(methylamino)riboflavin = S-adenosyl-L-homocysteine + roseoflavin

Glossary: roseoflavin = 8-demethyl-8-(dimethylamino)riboflavin

Other name(s): rosA (gene name)

Systematic name: S-adenosyl-L-methionine:8-amino-8-demethylriboflavin N,N-dimethyltransferase

Comments: The enzyme, characterized from the soil bacterium Streptomyces davawensis, catalyses the last two steps in the biosynthesis of the antibiotic roseoflavin.

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

References:

1. Jankowitsch, F., Kuhm, C., Kellner, R., Kalinowski, J., Pelzer, S., Macheroux, P. and Mack, M. A novel N,N-8-amino-8-demethyl-D-riboflavin dimethyltransferase (RosA) catalyzing the two terminal steps of roseoflavin biosynthesis in Streptomyces davawensis. J. Biol. Chem. 286 (2011) 38275-38285. [PMID: 21911488]

2. Tongsook, C., Uhl, M.K., Jankowitsch, F., Mack, M., Gruber, K. and Macheroux, P. Structural and kinetic studies on RosA, the enzyme catalysing the methylation of 8-demethyl-8-amino-D-riboflavin to the antibiotic roseoflavin. FEBS J. 283 (2016) 1531-1549. [PMID: 26913589]

[EC 2.1.1.343 created 2017]

EC 2.1.1.344

Accepted name: ornithine lipid N-methyltransferase

Reaction: 3 S-adenosyl-L-methionine + an ornithine lipid = 3 S-adenosyl-L-homocysteine + an N,N,N-trimethylornithine lipid (overall reaction)
(1a) S-adenosyl-L-methionine + an ornithine lipid = S-adenosyl-L-homocysteine + an N-methylornithine lipid
(1b) S-adenosyl-L-methionine + an N-methylornithine lipid = S-adenosyl-L-homocysteine + an N,N-dimethylornithine lipid
(1c) S-adenosyl-L-methionine + an N,N-dimethylornithine lipid = S-adenosyl-L-homocysteine + an N,N,N-trimethylornithine lipid

Glossary: an ornithine lipid = an Nα-[(3R)-3-(acyloxy)acyl]-L-ornithine

Other name(s): olsG (gene name)

Systematic name: S-adenosyl-L-methionine:ornithine lipid N-methyltransferase

Comments: The enzyme, characterized from the bacterium Singulisphaera acidiphila, catalyses three successive methylations of the terminal δ-nitrogen in ornithine lipids.

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

References:

1. Escobedo-Hinojosa, W.I., Vences-Guzman, M.A., Schubotz, F., Sandoval-Calderon, M., Summons, R.E., Lopez-Lara, I.M., Geiger, O. and Sohlenkamp, C. OlsG (Sinac_1600) is an ornithine lipid N-methyltransferase from the planctomycete Singulisphaera acidiphila. J. Biol. Chem. 290 (2015) 15102-15111. [PMID: 25925947]

[EC 2.1.1.344 created 2017]

EC 2.1.1.345

Accepted name: psilocybin synthase

Reaction: 2 S-adenosyl-L-methionine + 4-hydroxytryptamine 4-phosphate = 2 S-adenosyl-L-homocysteine + psilocybin (overall reaction)
(1a) S-adenosyl-L-methionine + 4-hydroxytryptamine 4-phosphate = S-adenosyl-L-homocysteine + 4-hydroxy-N-methyltryptamine 4-phosphate
(1b) S-adenosyl-L-methionine + 4-hydroxy-N-methyltryptamine 4-phosphate = S-adenosyl-L-homocysteine + psilocybin

For diagram of reaction click here

Glossary: psilocybin = 3-[2-(dimethylamino)ethyl]-1H-indol-4-yl phosphate

Other name(s): PsiM

Systematic name: S-adenosyl-L-methionine:4-hydroxytryptamine-4-phosphate N,N-dimethyltransferase

Comments: Isolated from the fungus Psilocybe cubensis. The product, psilocybin, is a psychoactive compound.

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

References:

1. Fricke, J., Blei, F. and Hoffmeister, D. Enzymatic synthesis of psilocybin. Angew. Chem. Int. Ed. Engl. 56 (2017) 12352-12355. [PMID: 28763571]

[EC 2.1.1.345 created 2017]

EC 2.1.1.346

Accepted name: U6 snRNA m6A methyltransferase

Reaction: S-adenosyl-L-methionine + adenine in U6 snRNA = S-adenosyl-L-homocysteine + N6-methyladenine in U6 snRNA

Other name(s): METTL16 (gene name)

Systematic name: S-adenosyl-L-methionine:adenine in U6 snRNA methyltransferase

Comments: This enzyme, found in vertebrates, methylates a specific adenine in a hairpin structure of snRNA. The effects of the binding of the methyltransferase to its substrate is important for the regulation of the activity of an isoform of EC 2.5.1.6, methionine adenosyltransferase, that produces S-adenosyl-L-methionine [1,2]. The enzyme also binds (and maybe methylates) the lncRNAs XIST and MALAT1 as well as a number of pre-mRNAs at specific positions often found in the intronic regions [2].

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

References:

1. Pendleton, K.E., Chen, B., Liu, K., Hunter, O.V., Xie, Y., Tu, B.P. and Conrad, N.K. The U6 snRNA m6A methyltransferase METTL16 regulates SAM synthetase intron retention. Cell 169 (2017) 824-835.e14. [PMID: 28525753]

2. Warda, A.S., Kretschmer, J., Hackert, P., Lenz, C., Urlaub, H., Hobartner, C., Sloan, K.E. and Bohnsack, M.T. Human METTL16 is a N6-methyladenosine (m6A) methyltransferase that targets pre-mRNAs and various non-coding RNAs. EMBO Rep. 18 (2017) 2004-2014. [PMID: 29051200]

[EC 2.1.1.346 created 2018]

EC 2.1.1.347

Accepted name: (+)-O-methylkolavelool synthase

Reaction: S-adenosyl-L-methionine + (+)-kolavelool = S-adenosyl-L-homocysteine + (+)-O-methylkolavelool

For diagram of reaction click here.

Other name(s): Haur_2147 (locus name)

Systematic name: S-adenosyl-L-methionine:(+)-kolavelool O-methyltransferase

Comments: Isolated from the bacterium Herpetosiphon aurantiacus.

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

References:

1. Nakano, C., Oshima, M., Kurashima, N. and Hoshino, T. Identification of a new diterpene biosynthetic gene cluster that produces O-methylkolavelool in Herpetosiphon aurantiacus. Chembiochem 16 (2015) 772-781. [PMID: 25694050]

[EC 2.1.1.347 created 2018]

EC 2.1.1.348

Accepted name: mRNA m6A methyltransferase

Reaction: S-adenosyl-L-methionine + adenine in mRNA = S-adenosyl-L-homocysteine + N6-methyladenine in mRNA

Other name(s): METTL3 (gene name); METTL14 (gene name)

Systematic name: S-adenosyl-L-methionine:adenine in mRNA methyltransferase

Comments: This enzyme, found in eukaryotes, methylates adenines in mRNA with the consensus sequence RRACH.

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

References:

1. Liu, J., Yue, Y., Han, D., Wang, X., Fu, Y., Zhang, L., Jia, G., Yu, M., Lu, Z., Deng, X., Dai, Q., Chen, W. and He, C. A METTL3-METTL14 complex mediates mammalian nuclear RNA N6-adenosine methylation. Nat. Chem. Biol. 10 (2014) 93-95. [PMID: 24316715]

2. Wang, X., Huang, J., Zou, T. and Yin, P. Human m6A writers: Two subunits, 2 roles. RNA Biol. 14 (2017) 300-304. [PMID: 28121234]

[EC 2.1.1.348 created 2018]

EC 2.1.1.349

Accepted name: toxoflavin synthase

Reaction: (1) S-adenosyl-L-methionine + 1,6-didemethyltoxoflavin = S-adenosyl-L-homocysteine + reumycin
(2) S-adenosyl-L-methionine + reumycin = S-adenosyl-L-homocysteine + toxoflavin

For diagram of reaction click here.

Glossary: reumycin = 1-demethyltoxoflavin
toxoflavin = 1,6-dimethylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione

Other name(s): toxA (gene name)

Systematic name: S-adenosyl-L-methionine:1,6-didemethyltoxoflavin N1,N6-dimethyltransferase (toxoflavin-forming)

Comments: The enzyme is a dual-specificity methyltransferase that catalyses the last two steps of toxoflavin biosynthesis. Toxoflavin is a major virulence factor of several bacterial crop pathogens.

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

References:

1. Fenwick, M.K., Philmus, B., Begley, T.P. and Ealick, S.E. Burkholderia glumae ToxA Is a dual-specificity methyltransferase that catalyzes the last two steps of toxoflavin biosynthesis. Biochemistry 55 (2016) 2748-2759. [PMID: 27070241]

[EC 2.1.1.349 created 2018]

EC 2.1.1.350

Accepted name: menaquinone C8-methyltransferase

Reaction: (1) 2 S-adenosyl-L-methionine + a menaquinone + reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + an 8-methylmenaquinone + oxidized flavodoxin
(2) 2 S-adenosyl-L-methionine + a 2-demethylmenaquinone + reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a 2-demethyl-8-methylmenaquinone + oxidized flavodoxin

For diagram of reaction click here

Other name(s): mqnK (gene name); menK (gene name)

Systematic name: S-adenosyl-L-methionine:menaquinone C8-methyltransferase

Comments: The enzyme, found in a wide range of bacteria and archaea, is a radical SAM (AdoMet) enzyme that utilizes two molecules of S-adenosyl-L-methionine, one as the methyl group donor, and one for the creation of a 5'-deoxyadenosine radical that drives the reaction forward.

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

References:

1. Hein, S., Klimmek, O., Polly, M., Kern, M. and Simon, J. A class C radical S-adenosylmethionine methyltransferase synthesizes 8-methylmenaquinone. Mol. Microbiol. 104 (2017) 449-462. [PMID: 28164386]

[EC 2.1.1.350 created 2018]

EC 2.1.1.351

= Accepted name: nocamycin O-methyltransferase

Reaction: S-adenosyl-L-methionine + nocamycin E = S-adenosyl-L-homocysteine + nocamycin I

For diagram of reaction click here

Glossary: nocamycin E = (2R,3S,3aS,5R,6R,7S,9aS)-5-[(2R,3E,5E)-7-hydroxy-4-methyl-7-(2,4-dioxopyrroliden-3-ylidene)hepta-3,5-dien-2-yl]-2,6,9a-trimethyl-8-oxooctahydro-3a,7-epoxyfuro[3,2-b]oxocine-3-carboxylate
nocamycin I = methyl (2R,3S,3aS,5R,6R,7S,9aS)-5-[(2R,3E,5E)-7-hydroxy-4-methyl-7-(2,4-dioxopyrroliden-3-ylidene)hepta-3,5-dien-2-yl]-2,6,9a-trimethyl-8-oxooctahydro-3a,7-epoxyfuro[3,2-b]oxocine-3-carboxylate

Other name(s): ncmP (gene name)

Systematic name: S-adenosyl-L-methionine:nocamycin E O-methyltransferase

Comments: The enzyme, isolated from the bacterium Saccharothrix syringae, is involved in the biosynthesis of nocamycin I and nocamycin II.

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

References:

1. Mo, X., Gui, C. and Wang, Q. Elucidation of a carboxylate O-methyltransferase NcmP in nocamycin biosynthetic pathway. Bioorg. Med. Chem. Lett. 27 (2017) 4431-4435. [PMID: 28818448]

[EC 2.1.1.351 created 2018]

EC 2.1.1.352

Accepted name: 3-O-acetyl-4'-O-demethylpapaveroxine 4'-O-methyltransferase

Reaction: S-adenosyl-L-methionine + 3-O-acetyl-4'-O-demethylpapaveroxine = S-adenosyl-L-homocysteine + 3-O-acetylpapaveroxine

Glossary: 3-O-acetyl-4'-O-demethylpapaveroxine = 6-{(S)-acetoxy[(5R)-4-hydroxy-6-methyl-5,6,7,8-tetrahydro[1,3]dioxolo[4,5-g]isoquinolin-5-yl]methyl}-2,3-dimethoxybenzaldehyde
3-O-acetylpapaveroxine = 6-{(S)-acetoxy[(5R)-4-methoxy-6-methyl-5,6,7,8-tetrahydro[1,3]dioxolo[4,5-g]isoquinolin-5-yl]methyl}-2,3-dimethoxybenzaldehyde

For diagram of reaction click here.

Systematic name: S-adenosyl-L-methionine:3-O-acetyl-4'-O-demethylpapaveroxine 4'-O-methyltransferase

Comments: This activity is part of the noscapine biosynthesis pathway, as characterized in the plant Papaver somniferum (opium poppy). It is catalysed by heterodimeric complexes of the OMT2 gene product and the product of either OMT3 or 6OMT. OMT2 is the catalytic subunit in both complexes.

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

References:

1. Li, Y. and Smolke, C.D. Engineering biosynthesis of the anticancer alkaloid noscapine in yeast. Nat Commun 7 (2016) 12137. [PMID: 27378283]

2. Park, M.R., Chen, X., Lang, D.E., Ng, K.KS. and Facchini, P.J. Heterodimeric O-methyltransferases involved in the biosynthesis of noscapine in opium poppy. Plant J. 95 (2018) 252-267. [PMID: 29723437]

[EC 2.1.1.352 created 2018]

EC 2.1.1.353

Accepted name: demethylluteothin O-methyltransferase

Reaction: S-adenosyl-L-methionine + demethylluteothin = S-adenosyl-L-homocysteine + luteothin

For diagram of reaction click here.

Glossary: luteothin = 2-[(3E,5E)-3,5-dimethyl-6-(4-nitrophenyl)hexa-3,5-dien-1-yl]-6-methoxy-3,5-dimethyl-4H-pyran-4-one
aureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E)-2-methyl-3-(4-nitrophenyl)prop-2-en-1-ylidene]oxolan-2-yl]-4H-pyran-4-one
spectinabilin = neoaureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E,4E,6E)-2,4,6-trimethyl-7-(4-nitrophenyl)hepta-2,4,6-trien-1-ylidene]oxolan-2-yl]-4H-pyran-4-one

Other name(s): aurI (gene name)

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

Comments: The enzyme, characterized from the bacterium Streptomyces thioluteus, participates in the biosynthesis of the antibiotic aureothin. An orthologous enzyme in the bacteria Streptomyces orinoci and Streptomyces spectabilis catalyses a similar reaction in the biosynthesis of spectinabilin.

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

References:

1. He, J., Muller, M. and Hertweck, C. Formation of the aureothin tetrahydrofuran ring by a bifunctional cytochrome P450 monooxygenase. J. Am. Chem. Soc. 126 (2004) 16742-16743. [PMID: 15612710]

2. Muller, M., He, J. and Hertweck, C. Dissection of the late steps in aureothin biosynthesis. Chembiochem 7 (2006) 37-39. [PMID: 16292785]

[EC 2.1.1.353 created 2019]

EC 2.1.1.354

Accepted name: histone H3 lysine-4 N-trimethyltransferase

Reaction: 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4 (overall reaction)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine4

Other name(s): KMT2A (gene name); KMT2B (gene name); KMT2C (gene name); KMT2D (gene name); KMT2E (gene name); KMT2F (gene name); KMT2G (gene name); KMT2H (gene name); KMT3C (gene name); KMT3D (gene name); KMT3E (gene name); KMT7 (gene name); PRDM7 (gene name); PRDM9 (gene name); MLL1 (gene name); MLL2 (gene name); MLL3 (gene name); MLL4 (gene name); MLL5 (gene name); SETD1A (gene name); ASH1L (gene name); SMYD1 (gene name); SMYD2 (gene name); SMYD3 (gene name); SET7/9 (gene name)

Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine4 N6-methyltransferase

Comments: This entry describes several enzymes that successively methylate the L-lysine4 residue of histone H3 (H3K4), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. In most cases the trimethylation of this position is associated with gene activation. Unlike the other enzymes, KMT7 catalyses only monomethylation.

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

References:

1. Nakamura, T., Mori, T., Tada, S., Krajewski, W., Rozovskaia, T., Wassell, R., Dubois, G., Mazo, A., Croce, C.M. and Canaani, E. ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation. Mol. Cell 10 (2002) 1119-1128. [PMID: 12453419]

2. Xiao, B., Jing, C., Wilson, J.R., Walker, P.A., Vasisht, N., Kelly, G., Howell, S., Taylor, I.A., Blackburn, G.M. and Gamblin, S.J. Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature 421 (2003) 652-656. [PMID: 12540855]

3. Hamamoto, R., Furukawa, Y., Morita, M., Iimura, Y., Silva, F.P., Li, M., Yagyu, R. and Nakamura, Y. SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat. Cell Biol. 6 (2004) 731-740. [PMID: 15235609]

4. Blazer, L.L., Lima-Fernandes, E., Gibson, E., Eram, M.S., Loppnau, P., Arrowsmith, C.H., Schapira, M. and Vedadi, M. PR domain-containing protein 7 (PRDM7) is a histone 3 lysine 4 trimethyltransferase. J. Biol. Chem 291 (2016) 13509-13519. [PMID: 27129774]

[EC 2.1.1.354 created 2019]

EC 2.1.1.355

Accepted name: histone H3 lysine-9 N-trimethyltransferase

Reaction: 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 (overall reaction)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9

Other name(s): KMT1A (gene name); KMT1B (gene name); KMT1C (gene name); KMT1D (gene name); KMT1E (gene name); KMT1F (gene name); MT8 (gene name); SUV39H1 (gene name); G9A (gene name); EHMT1 (gene name); PRDM2 (gene name)

Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine9 N6-methyltransferase

Comments: This entry describes several enzymes that successively methylate the L-lysine9 residue of histone H3 (H3K9), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. In general, the methylation of H3K9 leads to transcriptional repression of the affected target genes.

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

References:

1. O'Carroll, D., Scherthan, H., Peters, A.H., Opravil, S., Haynes, A.R., Laible, G., Rea, S., Schmid, M., Lebersorger, A., Jerratsch, M., Sattler, L., Mattei, M.G., Denny, P., Brown, S.D., Schweizer, D. and Jenuwein, T. Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression. Mol. Cell Biol. 20 (2000) 9423-9433. [PMID: 11094092]

2. Schotta, G., Ebert, A., Krauss, V., Fischer, A., Hoffmann, J., Rea, S., Jenuwein, T., Dorn, R. and Reuter, G. Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing. EMBO J. 21 (2002) 1121-1131. [PMID: 11867540]

3. Tachibana, M., Sugimoto, K., Nozaki, M., Ueda, J., Ohta, T., Ohki, M., Fukuda, M., Takeda, N., Niida, H., Kato, H. and Shinkai, Y. G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev. 16 (2002) 1779-1791. [PMID: 12130538]

4. Schultz, D.C., Ayyanathan, K., Negorev, D., Maul, G.G. and Rauscher, F.J., 3rd. SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 16 (2002) 919-932. [PMID: 11959841]

5. Kim, K.C., Geng, L. and Huang, S. Inactivation of a histone methyltransferase by mutations in human cancers. Cancer Res. 63 (2003) 7619-7623. [PMID: 14633678]

6. Wu, H., Min, J., Lunin, V.V., Antoshenko, T., Dombrovski, L., Zeng, H., Allali-Hassani, A., Campagna-Slater, V., Vedadi, M., Arrowsmith, C.H., Plotnikov, A.N. and Schapira, M. Structural biology of human H3K9 methyltransferases. PLoS One 5 (2010) e8570. [PMID: 20084102]

[EC 2.1.1.355 created 2019]

EC 2.1.1.356

Accepted name: histone H3 lysine27 N-trimethyltransferase

Reaction: 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27 (overall reaction)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27

Other name(s): KMT6A (gene name); KMT6B (gene name); EZH1 (gene name); EZH2 (gene name)

Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine27 N6-methyltransferase

Comments: This entry describes enzymes that successively methylate the L-lysine27 residue of histone H3 (H3K27), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. The methylation of lysine27 leads to transcriptional repression of the affected target genes. The enzyme associates with other proteins to form a complex that is essential for activity. The enzyme can also methylate some non-histone proteins.

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

References:

1. Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R.S. and Zhang, Y. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298 (2002) 1039-1043. [PMID: 12351676]

2. Kuzmichev, A., Nishioka, K., Erdjument-Bromage, H., Tempst, P. and Reinberg, D. Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev. 16 (2002) 2893-2905. [PMID: 12435631]

3. Kirmizis, A., Bartley, S.M., Kuzmichev, A., Margueron, R., Reinberg, D., Green, R. and Farnham, P.J. Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27. Genes Dev. 18 (2004) 1592-1605. [PMID: 15231737]

4. Schlesinger, Y., Straussman, R., Keshet, I., Farkash, S., Hecht, M., Zimmerman, J., Eden, E., Yakhini, Z., Ben-Shushan, E., Reubinoff, B.E., Bergman, Y., Simon, I. and Cedar, H. Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer. Nat. Genet. 39 (2007) 232-236. [PMID: 17200670]

5. Shen, X., Liu, Y., Hsu, Y.J., Fujiwara, Y., Kim, J., Mao, X., Yuan, G.C. and Orkin, S.H. EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency. Mol. Cell 32 (2008) 491-502. [PMID: 19026780]

6. Ezhkova, E., Lien, W.H., Stokes, N., Pasolli, H.A., Silva, J.M. and Fuchs, E. EZH1 and EZH2 cogovern histone H3K27 trimethylation and are essential for hair follicle homeostasis and wound repair. Genes Dev. 25 (2011) 485-498. [PMID: 21317239]

[EC 2.1.1.356 created 2019]

EC 2.1.1.357

Accepted name: histone H3 lysine36 N-dimethyltransferase

Reaction: 2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = 2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36 (overall reaction)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36

Other name(s): KMT3B (gene name); KMT3C (gene name); NSD2 (gene name); NSD3 (gene name); SETMAR (gene name); WHSC1 (gene name)

Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine36 N6-dimethyltransferase

Comments: This entry describes a group of metazoan enzymes that catalyse two successive methylations of lysine 36 of histone H3 (H3K36), forming mono- and dimethylated forms. These modifications influence the binding of chromatin-associated proteins. The product can be further methylated to the trimethyl form by EC 2.1.1.358, histone H3 dimethyl-L-lysine36 N-methyltransferase. The yeast SET2 enzyme can catalyse all three methylations (see EC 2.1.1.359, histone H3 lysine36 N-trimethyltransferase).

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

References:

1. Fnu, S., Williamson, E.A., De Haro, L.P., Brenneman, M., Wray, J., Shaheen, M., Radhakrishnan, K., Lee, S.H., Nickoloff, J.A. and Hromas, R. Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining. Proc. Natl Acad. Sci. USA 108 (2011) 540-545. [PMID: 21187428]

2. Kuo, A.J., Cheung, P., Chen, K., Zee, B.M., Kioi, M., Lauring, J., Xi, Y., Park, B.H., Shi, X., Garcia, B.A., Li, W. and Gozani, O. NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming. Mol. Cell 44 (2011) 609-620. [PMID: 22099308]

3. Qiao, Q., Li, Y., Chen, Z., Wang, M., Reinberg, D. and Xu, R.M. The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation. J. Biol. Chem 286 (2011) 8361-8368. [PMID: 21196496]

4. Wagner, E.J. and Carpenter, P.B. Understanding the language of Lys36 methylation at histone H3. Nat. Rev. Mol. Cell. Biol. 13 (2012) 115-126. [PMID: 22266761]

[EC 2.1.1.357 created 2019]

EC 2.1.1.358

Accepted name: histone H3 dimethyl-L-lysine36 N-methyltransferase

Reaction: S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36

Other name(s): KMT3A (gene name); SETD2 (gene name)

Systematic name: S-adenosyl-L-methionine:[histone H3]-N6,N6-dimethyl-L-lysine36 N6-methyltransferase

Comments: The enzyme, found in metazoa, methylates a dimethylated L-lysine36 residue of histone H3 (H3K36), which has been methylated previously by EC 2.1.1.357, histone H3 lysine36 N-dimethyltransferase. The homologous enzyme from yeast catalyses all three methylations (see EC 2.1.1.359, histone H3 lysine36 N-trimethyltransferase).

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

References:

1. Kizer, K.O., Phatnani, H.P., Shibata, Y., Hall, H., Greenleaf, A.L. and Strahl, B.D. A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation. Mol. Cell Biol. 25 (2005) 3305-3316. [PMID: 15798214]

2. Yuan, W., Xie, J., Long, C., Erdjument-Bromage, H., Ding, X., Zheng, Y., Tempst, P., Chen, S., Zhu, B. and Reinberg, D. Heterogeneous nuclear ribonucleoprotein L Is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo. J. Biol. Chem 284 (2009) 15701-15707. [PMID: 19332550]

3. Wagner, E.J. and Carpenter, P.B. Understanding the language of Lys36 methylation at histone H3. Nat. Rev. Mol. Cell. Biol. 13 (2012) 115-126. [PMID: 22266761]

[EC 2.1.1.358 created 2019]

EC 2.1.1.359

Accepted name: histone H3 lysine36 N-trimethyltransferase

Reaction: 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36 (overall reaction)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36

Other name(s): SET2 (gene name)

Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine36 N6-trimethyltransferase

Comments: The enzyme, characterized from yeast, catalyses the successive methylation of lysine36 of histone H3 (H3K36), forming the trimethylated form. These modifications influence the binding of chromatin-associated proteins. The enzyme couples the methylation reactions with transcriptional elongation through an interaction with the large subunit of RNA polymerase II. In mammals this activity is catalysed by two different enzymes, EC 2.1.1.357, histone H3 lysine36 N-dimethyltransferase and EC 2.1.1.358, histone H3 dimethyl-L-lysine36 N-methyltransferase.

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

References:

1. Strahl, B.D., Grant, P.A., Briggs, S.D., Sun, Z.W., Bone, J.R., Caldwell, J.A., Mollah, S., Cook, R.G., Shabanowitz, J., Hunt, D.F. and Allis, C.D. Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression. Mol. Cell Biol. 22 (2002) 1298-1306. [PMID: 11839797]

2. Landry, J., Sutton, A., Hesman, T., Min, J., Xu, R.M., Johnston, M. and Sternglanz, R. Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae. Mol. Cell Biol. 23 (2003) 5972-5978. [PMID: 12917322]

3. Morris, S.A., Shibata, Y., Noma, K., Tsukamoto, Y., Warren, E., Temple, B., Grewal, S.I. and Strahl, B.D. Histone H3 K36 methylation is associated with transcription elongation in Schizosaccharomyces pombe. Eukaryot Cell 4 (2005) 1446-1454. [PMID: 16087749]

4. Lin, L.J., Minard, L.V., Johnston, G.C., Singer, R.A. and Schultz, M.C. Asf1 can promote trimethylation of H3 K36 by Set2. Mol. Cell Biol. 30 (2010) 1116-1129. [PMID: 20048053]

[EC 2.1.1.359 created 2019]

EC 2.1.1.360

Accepted name: histone H3 lysine79 N-trimethyltransferase

Reaction: 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine79 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine79 (overall reaction)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine79 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine79
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine79 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine79
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine79 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine-79

Other name(s): DOT1L (gene name); KMT4 (gene name)

Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine79 N6-trimethyltransferase

Comments: The enzyme successively methylates the L-lysine79 residue of histone H3 (H3K79), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. This is the only known methylation event of a lysine residue within the core region of a histone, as all other such modifications occur at the tail.

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

References:

1. Feng, Q., Wang, H., Ng, H.H., Erdjument-Bromage, H., Tempst, P., Struhl, K. and Zhang, Y. Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr. Biol. 12 (2002) 1052-1058. [PMID: 12123582]

2. Ng, H.H., Feng, Q., Wang, H., Erdjument-Bromage, H., Tempst, P., Zhang, Y. and Struhl, K. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev. 16 (2002) 1518-1527. [PMID: 12080090]

3. Min, J., Feng, Q., Li, Z., Zhang, Y. and Xu, R.M. Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell 112 (2003) 711-723. [PMID: 12628190]

4. Steger, D.J., Lefterova, M.I., Ying, L., Stonestrom, A.J., Schupp, M., Zhuo, D., Vakoc, A.L., Kim, J.E., Chen, J., Lazar, M.A., Blobel, G.A. and Vakoc, C.R. DOT1L/KMT4 recruitment and H3K79 methylation are ubiquitously coupled with gene transcription in mammalian cells. Mol. Cell Biol. 28 (2008) 2825-2839. [PMID: 18285465]

[EC 2.1.1.360 created 2019]

EC 2.1.1.361

Accepted name: histone H4 lysine20 N-methyltransferase

Reaction: S-adenosyl-L-methionine + a [histone H4]-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine-20

Other name(s): KMT5A (gene name); SET8 (gene name); PR-SET7 (gene name)

Systematic name: S-adenosyl-L-methionine:[histone H4]-L-lysine20 N6-methyltransferase

Comments: The enzyme catalyses the monomethylation of the L-lysine20 residue of histone H4 (H4K20). This event is usually followed by further methylation by EC 2.1.1.362, histone H4 N-methyl-L-lysine20 N-methyltransferase. This enzyme plays a pivotal role in DNA replication. Activity is high during the G2 and M phases, but declines significantly during G1 and S phases. Mutations in the enzyme have severe consequences, including DNA double-strand breaks, activation of DNA damage checkpoints, defective cell cycle progression, and reduced cell proliferation.

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

References:

1. Fang, J., Feng, Q., Ketel, C.S., Wang, H., Cao, R., Xia, L., Erdjument-Bromage, H., Tempst, P., Simon, J.A. and Zhang, Y. Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase. Curr. Biol. 12 (2002) 1086-1099. [PMID: 12121615]

2. Nishioka, K., Rice, J.C., Sarma, K., Erdjument-Bromage, H., Werner, J., Wang, Y., Chuikov, S., Valenzuela, P., Tempst, P., Steward, R., Lis, J.T., Allis, C.D. and Reinberg, D. PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin. Mol. Cell 9 (2002) 1201-1213. [PMID: 12086618]

3. Jorgensen, S., Elvers, I., Trelle, M.B., Menzel, T., Eskildsen, M., Jensen, O.N., Helleday, T., Helin, K. and Sorensen, C.S. The histone methyltransferase SET8 is required for S-phase progression. J. Cell Biol. 179 (2007) 1337-1345. [PMID: 18166648]

4. Oda, H., Okamoto, I., Murphy, N., Chu, J., Price, S.M., Shen, M.M., Torres-Padilla, M.E., Heard, E. and Reinberg, D. Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development. Mol. Cell Biol. 29 (2009) 2278-2295. [PMID: 19223465]

5. Jorgensen, S., Schotta, G. and Sorensen, C.S. Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity. Nucleic Acids Res. 41 (2013) 2797-2806. [PMID: 23345616]

[EC 2.1.1.361 created 2019]

EC 2.1.1.362

Accepted name: histone H4 N-methyl-L-lysine20 N-methyltransferase

Reaction: S-adenosyl-L-methionine + a [histone H4]-N6-methyl-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6,N6-dimethyl-L-lysine20

Other name(s): KMT5B (gene name); KMT5C (gene name); SUV420H1 (gene name); SUV420H2 (gene name)

Systematic name: S-adenosyl-L-methionine:[histone H4]-N6-methyl-L-lysine20 N6-methyltransferase

Comments: This entry describes a group of enzymes that catalyse a single methylation of monomethylated lysine 20 of histone H4 (H4K20m1, generated by EC 2.1.1.361, histone H4 lysine20 N-methyltransferase), forming the dimethylated form. This modification is broadly distributed across the genome and is likely important for general chromatin-mediated processes. The double-methylated form of lysine20 in histone H4 is the most abundant methylation state of this residue and is found on ~80% of all histone H4 molecules. Full activity of the enzyme requires that the lysine at position 9 of histone H3 is trimethylated.

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

References:

1. Schotta, G., Lachner, M., Sarma, K., Ebert, A., Sengupta, R., Reuter, G., Reinberg, D. and Jenuwein, T. A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev. 18 (2004) 1251-1262. [PMID: 15145825]

2. Jorgensen, S., Schotta, G. and Sorensen, C.S. Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity. Nucleic Acids Res. 41 (2013) 2797-2806. [PMID: 23345616]

3. Wu, H., Siarheyeva, A., Zeng, H., Lam, R., Dong, A., Wu, X.H., Li, Y., Schapira, M., Vedadi, M. and Min, J. Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2. FEBS Lett. 587 (2013) 3859-3868. [PMID: 24396869]

4. Southall, S.M., Cronin, N.B. and Wilson, J.R. A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases. Nucleic Acids Res. 42 (2014) 661-671. [PMID: 24049080]

5. Weirich, S., Kudithipudi, S. and Jeltsch, A. Specificity of the SUV4-20H1 and SUV4-20H2 protein lysine methyltransferases and methylation of novel substrates. J. Mol. Biol. 428 (2016) 2344-2358. [PMID: 27105552]

[EC 2.1.1.362 created 2019]

EC 2.1.1.363

Accepted name: pre-sodorifen synthase

Reaction: S-adenosyl-L-methionine + (2E,6E)-farnesyl diphosphate = S-adenosyl-L-homocysteine + pre-sodorifen diphosphate

Glossary: pre-sodorifen diphosphate = [(2E)-3-methyl-5-[(1S,4R,5R)-1,2,3,4,5-pentamethylcyclopent-2-en-1-yl]pent-2-en-1-yl phosphonato]oxyphosphonate
sodorifen = (1S,2S,4R,5S,8s)-1,2,4,5,6,7,8-heptamethyl-3-methylenebicyclo[3.2.1]oct-6-ene

Other name(s): sodC (gene name)

Systematic name: (2E,6E)-farnesyl diphosphate 10-C-methyltransferase (cyclyzing, pre-sodorifen diphosphate producing)

Comments: The enzyme, characterized from the bacterium Serratia plymuthica, participates in biosynthesis of sodorifen.

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

References:

1. Domik, D., Magnus, N. and Piechulla, B. Analysis of a new cluster of genes involved in the synthesis of the unique volatile organic compound sodorifen of Serratia plymuthica 4Rx13. FEMS Microbiol. Lett. 363(14) (2016) fnw139. [PMID: 27231241]

2. Schmidt, R., Jager, V., Zuhlke, D., Wolff, C., Bernhardt, J., Cankar, K., Beekwilder, J., Ijcken, W.V., Sleutels, F., Boer, W., Riedel, K. and Garbeva, P. Fungal volatile compounds induce production of the secondary metabolite sodorifen in Serratia plymuthica PRI-2C. Sci Rep 7 (2017) 862. [PMID: 28408760]

3. von Reuss, S., Domik, D., Lemfack, M.C., Magnus, N., Kai, M., Weise, T. and Piechulla, B. Sodorifen biosynthesis in the rhizobacterium Serratia plymuthica involves methylation and cyclization of MEP-derived farnesyl pyrophosphate by a SAM-dependent C-methyltransferase. J. Am. Chem. Soc. 140 (2018) 11855-11862. [PMID: 30133268]

[EC 2.1.1.363 created 2019]


Continued with EC 2.1.2.1 to EC 2.2.1.4
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