EC 2.1.1 Methyltransferases
EC 2.1.2 Hydroxymethyl-, Formyl- and Related Transferases
EC 2.1.3 Carboxyl- and Carbamoyltransferases
EC 2.1.4 Amidinotransferases
('Methyltransferase' may be replaced by 'transmethylase').
EC 2.1.1.1 nicotinamide N-methyltransferase
EC 2.1.1.2 guanidinoacetate N-methyltransferase
EC 2.1.1.3 thetin—homocysteine S-methyltransferase
EC 2.1.1.4 acetylserotonin O-methyltransferase
EC 2.1.1.5 betaine—homocysteine S-methyltransferase
EC 2.1.1.6 catechol O-methyltransferase
EC 2.1.1.7 nicotinate N-methyltransferase
EC 2.1.1.8 histamine N-methyltransferase
EC 2.1.1.9 thiol S-methyltransferase
EC 2.1.1.10 homocysteine S-methyltransferase
EC 2.1.1.11 magnesium protoporphyrin IX methyltransferase
EC 2.1.1.12 methionine S-methyltransferase
EC 2.1.1.13 methionine synthase
EC 2.1.1.14 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase
EC 2.1.1.15 fatty-acid O-methyltransferase
EC 2.1.1.16 methylene-fatty-acyl-phospholipid synthase
EC 2.1.1.17 phosphatidylethanolamine N-methyltransferase
EC 2.1.1.18 polysaccharide O-methyltransferase
EC 2.1.1.19 trimethylsulfonium—tetrahydrofolate N-methyltransferase
EC 2.1.1.20 glycine N-methyltransferase
EC 2.1.1.21 methylamine—glutamate N-methyltransferase
EC 2.1.1.22 carnosine N-methyltransferase
EC 2.1.1.23 now covered by EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126
EC 2.1.1.24 now covered by EC 2.1.1.77, EC 2.1.1.80 and EC 2.1.1.100
EC 2.1.1.25 phenol O-methyltransferase
EC 2.1.1.26 iodophenol O-methyltransferase
EC 2.1.1.27 tyramine N-methyltransferase
EC 2.1.1.28 phenylethanolamine N-methyltransferase
EC 2.1.1.29 tRNA (cytosine-5-)-methyltransferase
EC 2.1.1.30 deleted
EC 2.1.1.31 tRNA (guanine-N1-)-methyltransferase
EC 2.1.1.32 tRNA (guanine-N2-)-methyltransferase
EC 2.1.1.33 tRNA (guanine-N7-)-methyltransferase
EC 2.1.1.34 tRNA guanosine-2'-O-methyltransferase
EC 2.1.1.35 tRNA (uracil-5-)-methyltransferase
EC 2.1.1.36 tRNA (adenine-N1-)-methyltransferase
EC 2.1.1.37 DNA (cytosine-5-)-methyltransferase
EC 2.1.1.38 O-demethylpuromycin O-methyltransferase
EC 2.1.1.39 inositol 3-methyltransferase
EC 2.1.1.40 inositol 1-methyltransferase
EC 2.1.1.41 24-sterol C-methyltransferase
EC 2.1.1.42 luteolin O-methyltransferase
EC 2.1.1.43 histone-lysine N-methyltransferase
EC 2.1.1.44 dimethylhistidine N-methyltransferase
EC 2.1.1.45 thymidylate synthase
EC 2.1.1.46 isoflavone 4'-O-methyltransferase
EC 2.1.1.47 indolepyruvate C-methyltransferase
EC 2.1.1.48 rRNA (adenine-N6-)-methyltransferase
EC 2.1.1.49 amine N-methyltransferase
EC 2.1.1.50 loganate O-methyltransferase
See the following files for:
EC 2.1.1.51 to EC 2.1.1.100
EC 2.1.1.101 to EC 2.1.1.163
Accepted name: nicotinamide N-methyltransferase
Reaction: S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + 1-methylnicotinamide
Other name(s): nicotinamide methyltransferase
Systematic name: S-adenosyl-L-methionine:nicotinamide N-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9029-74-7
References:
1. Cantoni, G.L. Methylation of nicotinamide with a soluble enzyme system from rat liver. J. Biol. Chem. 189 (1951) 203-216.
Accepted name: guanidinoacetate N-methyltransferase
Reaction: S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
For diagram of reaction click here.
Other name(s): GA methylpherase; guanidinoacetate methyltransferase; guanidinoacetate transmethylase; methionine-guanidinoacetic transmethylase; guanidoacetate methyltransferase
Systematic name: S-adenosyl-L-methionine:N-guanidinoacetate methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9029-75-8
References:
1. Cantoni, G.L. and Scarano, E. The formation of S-adenosylhomocysteine in enzymatic transmethylation reactions. J. Am. Chem. Soc. 76 (1954) 4744 only.
2. Cantoni, G.L. and Vignos, P.J. Enzymatic mechanism of creatine synthesis. J. Biol. Chem. 209 (1954) 647-659.
Accepted name: thetin—homocysteine S-methyltransferase
Reaction: dimethylsulfonioacetate + L-homocysteine = S-methylthioglycolate + L-methionine
Other name(s): dimethylthetin-homocysteine methyltransferase; thetin-homocysteine methylpherase
Systematic name: dimethylsulfonioacetate:L-homocysteine S-methyltransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, CAS registry number: 9029-76-9
References:
1. Klee, W.A., Richards, H.H. and Cantoni, G.L. The synthesis of methionine by enzymic transmethylation. VII. Existence of two separate homocysteine methylpherases on mammalian liver. Biochim. Biophys. Acta 54 (1961) 157-164.
2. Maw, G.A. Thetin-homocysteine transmethylase. A preliminary manometric study of the enzyme from rat liver. Biochem. J. 63 (1956) 116-124.
3. Maw, G.A. Thetin-homocysteine transmethylase. Some further characteristics of the enzyme from rat liver. Biochem. J. 70 (1958) 168-173.
Accepted name: acetylserotonin O-methyltransferase
Reaction: S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
Glossary entries:
Melatonin: N-acetyl-5-methoxytryptamine
Serotonin: 5-hydroxytryptamine
Tryptamine: 2-(1H-indol-3-yl)ethanamine
Other name(s): hydroxyindole methyltransferase; hydroxyindole O-methyltransferase; N-acetylserotonin O-methyltransferase; acetylserotonin methyltransferase
Systematic name: S-adenosyl-L-methionine:N-acetylserotonin O-methyltransferase
Comments: Some other hydroxyindoles also act as acceptor, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9029-77-0
References:
1. Axelrod, J. and Weissbach, H. Purification and properties of hydroxyindole-O-methyl transferase. J. Biol. Chem. 236 (1961) 211-213.
Accepted name: betaine—homocysteine S-methyltransferase
Reaction: trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine
Other name(s): betaine-homocysteine methyltransferase; betaine-homocysteine transmethylase
Systematic name: trimethylammonioacetate:L-homocysteine S-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9029-78-1
References:
1. Klee, W.A., Richards, H.H. and Cantoni, G.L. The synthesis of methionine by enzymic transmethylation. VII. Existence of two separate homocysteine methylpherases on mammalian liver. Biochim. Biophys. Acta 54 (1961) 157-164.
Accepted name: catechol O-methyltransferase
Reaction: S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
Other name(s): COMT I ; COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase
Systematic name: S-adenosyl-L-methionine:catechol O-methyltransferase
Comments: The mammalian enzyme acts more rapidly on catecholamines such as adrenaline or noradrenaline than on catechols.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9012-25-3
References:
1. Axelrod, J. and Tomchick, R. Enzymatic O-methylation of epinephrine and other catechols. J. Biol. Chem. 233 (1958) 702-705.
2. Gulliver, P.A. and Tipton, K.F. The purification and properties of pig brain catechol-O-methyltransferase. J. Neurochem. 32 (1979) 1525-1529. [PMID: 438821]
3. Huh, M.M.O. and Friedhof, A.J. Multiple molecular forms of catechol-O-methyltransferase. Evidence for two distinct forms, and their purification and physical characterization. J. Biol. Chem. 254 (1979) 299-308. [PMID: 762061]
Accepted name: nicotinate N-methyltransferase
Reaction: S-adenosyl-L-methionine + nicotinate = S-adenosyl-L-homocysteine + N-methylnicotinate
Other name(s): furanocoumarin 8-methyltransferase; furanocoumarin 8-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:nicotinate N-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9029-79-2
References:
1. Joshi, J.G. and Handler, P. Biosynthesis of trigonelline. J. Biol. Chem. 235 (1960) 2981-2983.
Accepted name: histamine N-methyltransferase
Reaction: S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + Nτ-methylhistamine
Other name(s): histamine 1-methyltransferase; histamine methyltransferase; histamine-methylating enzyme; imidazolemethyltransferase; S-adenosylmethionine-histamine N-methyltransferase
Systematic name: S-adenosyl-L-methionine:histamine N-tele-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9029-80-5
References:
1. Brown, D.D., Tomchick, R. and Axelrod, J. The distribution and properties of a histamine-methylating enzyme. J. Biol. Chem. 234 (1959) 2948-2950.
Accepted name: thiol S-methyltransferase
Reaction: S-adenosyl-L-methionine + a thiol = S-adenosyl-L-homocysteine + a thioether
Other name(s): S-methyltransferase; thiol methyltransferase; TMT
Systematic name: S-adenosyl-L-methionine:thiol S-methyltransferase
Comments: H2S and a variety of alkyl, aryl and heterocyclic thiols and hydroxy thiols can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, CAS registry number: 9029-81-6
References:
1. Borchardt, R.T. and Cheng, C.F. Purification and characterization of rat liver microsomal thiol methyltransferase. Biochim. Biophys. Acta 522 (1978) 340-353. [PMID: 623768]
2. Bremer, J. and Greenberg, D.M. Enzymic methylation of foreign sulfhydryl compounds Biochim. Biophys. Acta 46 (1961) 217-224.
3. Weisiger, R.A. and Jakoby, W.B. Thiol S-methyltransferase from rat liver. Arch. Biochem. Biophys. 196 (1979) 631-637. [PMID: 485170]
Accepted name: homocysteine S-methyltransferase
Reaction: S-adenosyl-L-methionine + L-homocysteine = S-adenosyl-L-homocysteine + L-methionine
Other name(s): S-adenosylmethionine homocysteine transmethylase; S-methylmethionine homocysteine transmethylase; adenosylmethionine transmethylase; methylmethionine:homocysteine methyltransferase; adenosylmethionine:homocysteine methyltransferase; homocysteine methylase; homocysteine methyltransferase; homocysteine transmethylase; L-homocysteine S-methyltransferase; S-adenosyl-L-methionine:L-homocysteine methyltransferase; S-adenosylmethionine-homocysteine transmethylase; S-adenosylmethionine:homocysteine methyltransferase
Systematic name: S-adenosyl-L-methionine:L-homocysteine S-methyltransferase
Comments: The bacterial enzyme uses S-methylmethionine as donor more actively than S-adenosylmethionine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, CAS registry number: 9012-40-2
References:
1. Balish, E. and Shapiro, S.K. Methionine biosynthesis in Escherichia coli: induction and repression of methylmethionine (or adenosylmethionine):homocysteine methyltransferase. Arch. Biochem. Biophys. 119 (1967) 62-68. [PMID: 4861151]
2. Shapiro, S.K. Adenosylmethionine-homocysteine transmethylase. Biochim. Biophys. Acta 29 (1958) 405-409.
3. Shapiro, S.K. and Yphantis, D.A. Assay of S-methylmethionine and S-adenosylmethionine homocysteine transmethylases. Biochim. Biophys. Acta 36 (1959) 241-244.
Accepted name: magnesium protoporphyrin IX methyltransferase
Reaction: S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
For diagram of reaction click here (chlorophyll biosynthesis).
Other name(s): Mg-protoporphyrin IX methyltransferase; S-adenosylmethionine-magnesium protoporphyrin methyltransferase; magnesium-protoporphyrin O-methyltransferase; (-)-S-adenosyl-L-methionine:magnesium-protoporphyrin IX methyltransferase; S-adenosyl-L-methionine:Mg protoporphyrin methyltransferase; S-adenosylmethioninemagnesium protoporphyrin methyltransferase; S-adenosyl-L-methionine:magnesium-protoporphyrin O-methyltransferase
Systematic name: S-adenosyl-L-methionine:magnesium-protoporphyrin-IX O-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9029-82-7
References:
1. Gibson, K.D., Neuberger, A. and Tait, G.H. Studies on the biosynthesis of porphyrin and bacteriochlorophyll by Rhodopseudomonas spheroides. 4. S-Adenosylmethioninemagnesium protoporphyrin methyltransferase. Biochem. J. 88 (1963) 325-334.
2. Shepherd, M., Reid, J.D. and Hunter, C.N. Purification and kinetic characterisation of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803. Biochem. J. 371 (2003) 351-360. [PMID: 12489983]
3. Bollivar, D.W., Jiang, Z.Y., Bauer, C.E. and Beale, S.I. Heterologous expression of the bchM gene product from Rhodobacter capsulatus and demonstration that it encodes S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase. J. Bacteriol. 176 (1994) 5290-5296. [PMID: 8071204]
4. Gibson, L.C. and Hunter, C.N. The bacteriochlorophyll biosynthesis gene, bchM, of Rhodobacter sphaeroides encodes S-adenosyl-L-methionine: Mg protoporphyrin IX methyltransferase. FEBS Lett. 352 (1994) 127-130. [PMID: 7925960]
5. Ebbon, J.G. and Tait, G.H. Studies on S-adenosylmethionine-magnesium protoporphyrin methyltransferase in Euglena gracilis strain Z. Biochem. J. 111 (1969) 573-582. [PMID: 5774480]
Accepted name: methionine S-methyltransferase
Reaction: S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine
Other name(s): S-adenosyl methionine:methionine methyl transferase; methionine methyltransferase; S-adenosylmethionine transmethylase; S-adenosylmethionine-methionine methyltransferase
Systematic name: S-adenosyl-L-methionine:L-methionine S-methyltransferase
Comments: Requires Zn2+ or Mn2+
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9027-77-4
References:
1. Karr, D. Tweto, J. and Albersheim, P. S-Adenosyl methionine: methionine methyl transferase from wheat germ. Arch. Biochem. Biophys. 121 (1967) 732-738. [PMID: 6078098]
Accepted name: methionine synthase
Reaction: 5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine
For diagram click here.
Other name(s): 5-methyltetrahydrofolate—homocysteine S-methyltransferase; 5-methyltetrahydrofolate—homocysteine transmethylase; N-methyltetrahydrofolate:L-homocysteine methyltransferase; N5-methyltetrahydrofolate methyltransferase; N5-methyltetrahydrofolate—homocysteine cobalamin methyltransferase; N5-methyltetrahydrofolic—homocysteine vitamin B12 transmethylase; B12 N5-methyltetrahydrofolate homocysteine methyltransferase; methyltetrahydrofolate—homocysteine vitamin B12 methyltransferase; tetrahydrofolate methyltransferase; tetrahydropteroylglutamate methyltransferase; tetrahydropteroylglutamic methyltransferase; vitamin B12 methyltransferase; cobalamin-dependent methionine synthase; methionine synthase (cobalamin-dependent); MetH
Systematic name: 5-methyltetrahydrofolate:L-homocysteine S-methyltransferase
Comments: Contains zinc and cobamide. The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II). Reactivation by reductive methylation is catalysed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system. For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8, [methionine synthase] reductase. In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2, ferredoxin—NADP+ reductase). Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase, which acts only on the triglutamate.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9033-23-2
References:
1. Burton, E.G. and Sakami, W. The formation of methionine from the monoglutamate form of methyltetrahydrofolate by higher plants. Biochem. Biophys. Res. Commun. 36 (1969) 228-234. [PMID: 5799642]
2. Foster, M.A., Dilworth, M.J. and Woods, D.D. Cobalamin and the synthesis of methionine by Escherichia coli. Nature 201 (1964) 39-42.
3. Guest, J.R., Friedman, S., Foster, M.A., Tejerina, G. and Woods, D.D. Transfer of the methyl group from N5-methyltetrahydrofolates to homocysteine in Escherichia coli. Biochem. J. 92 (1964) 497-504.
4. Loughlin, R.E., Elford, H.L. and Buchanan, J.M. Enzymatic synthesis of the methyl group of methionine. VII. Isolation of a cobalamin-containing transmethylase (5-methyltetrahydro-folate-homocysteine) from mammalian liver. J. Biol. Chem. 239 (1964) 2888-2895.
5. Taylor, R.T. Escherichia coli B N5-methyltetrahydrofolate-homocysteine cobalamin methyltransferase: gel-filtration behavior of apoenzyme and holoenzymes. Biochim. Biophys. Acta 242 (1971) 355-364. [PMID: 4946148]
6. Jarrett, J.T., Huang, S. and Matthews, R.G. Methionine synthase exists in two distinct conformations that differ in reactivity toward methyltetrahydrofolate, adenosylmethionine, and flavodoxin. Biochemistry 37 (1998) 5372-5382. [PMID: 9548919]
7. Peariso, K., Goulding, C.W., Huang, S., Matthews, R.G. and Penner-Hahn, J.E. Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: The role of zinc in the methylation of homocysteine. J. Am. Chem. Soc. 120 (1998) 8410-8416.
8. Hall, D.A., Jordan-Starck, T.C., Loo, R.O., Ludwig, M.L. and Matthews, R.G. Interaction of flavodoxin with cobalamin-dependent methionine synthase. Biochemistry 39 (2000) 10711-10719. [PMID: 10978155]
9. Bandarian, V., Pattridge, K.A., Lennon, B.W., Huddler, D.P., Matthews, R.G. and Ludwig, M.L. Domain alternation switches B12-dependent methionine synthase to the activation conformation. Nat. Struct. Biol. 9 (2002) 53-56. [PMID: 11731805]
Accepted name: 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase
Reaction: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine
Other name(s): tetrahydropteroyltriglutamate methyltransferase; homocysteine methylase; methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase; methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase; cobalamin-independent methionine synthase; methionine synthase (cobalamin-independent); MetE
Systematic name: 5-methyltetrahydropteroyltri-L-glutamate:L-homocysteine S-methyltransferase
Comments: Requires phosphate and contains zinc. The enzyme from Escherichia coli also requires a reducing system. Unlike EC 2.1.1.13, methionine synthase, this enzyme does not contain cobalamin.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9068-29-5
References:
1. Guest, J.R., Friedman, S., Foster, M.A., Tejerina, G. and Woods, D.D. Transfer of the methy grouup from N5-methyltetrahydrofolates to homocysteine in Escherichia coli. Biochem. J. 92 (1964) 497-504.
2. Whitfield, C.D., Steers, E.J., Jr. and Weissbach, H. Purification and properties of 5-methyltetrahydropteroyltriglutamate-homocysteine transmethylase. J. Biol. Chem. 245 (1970) 390-401. [PMID: 4904482]
3. Eichel, J., Gonzalez, J.C., Hotze, M., Matthews, R.G. and Schroder, J. Vitamin B12-independent methionine synthase from a higher-plant (Catharanthus roseus) - molecular characterization, regulation, heterologous expression, and enzyme properties. Eur. J. Biochem. 230 (1995) 1053-1058. [PMID: 7601135]
4. Gonzalez, J.C., Peariso, K., PennerHahn, J.E. and Matthews, R.G. Cobalamin-independent methionine synthase from Escherichia coli: A zinc metalloenzyme. Biochemistry 35 (1996) 12228-12234. [PMID: 8823155]
5. Peariso, K., Goulding, C.W., Huang, S., Matthews, R.G. and Penner-Hahn, J.E. Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: The role of zinc in the methylation of homocysteine. J. Am. Chem. Soc. 120 (1998) 8410-8416.
Accepted name: fatty-acid O-methyltransferase
Reaction: S-adenosyl-L-methionine + a fatty acid = S-adenosyl-L-homocysteine + a fatty acid methyl ester
Other name(s): fatty acid methyltransferase; fatty acid O-methyltransferase
Systematic name: S-adenosyl-L-methionine:fatty-acid O-methyltransferase
Comments: Oleic acid is the most effective fatty acid acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-89-6
References:
1. Akamatsu, Y. and Law, J.H. The enzymatic synthesis of fatty acid methyl esters by carboxyl group alkylation. J. Biol. Chem. 245 (1970) 709-713. [PMID: 4984625]
Accepted name: methylene-fatty-acyl-phospholipid synthase
Reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid methylene fatty acid
Other name(s): unsaturated-phospholipid methyltransferase
Systematic name: S-adenosyl-L-methionine:unsaturated-phospholipid methyltransferase (methenylating)
Comments: The enzyme transfers a methyl group to the 10-position of a δ-olefinic acyl chain in phosphatidylglycerol or phosphatidylinositol or, more slowly, phosphatidylethanolamine; subsequent proton transfer produces a 10-methylene group (cf. EC 2.1.1.79 cyclopropane-fatty-acyl-phospholipid synthase).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-90-9
References:
1. Akamatsu, Y. and Law, J.H. Enzymatic alkylenation of phospholipid fatty acid chains by extracts of Mycobacterium phlei. J. Biol. Chem. 245 (1970) 701-708. [PMID: 4313604]
Accepted name: phosphatidylethanolamine N-methyltransferase
Reaction: S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
Other name(s): PEMT; LMTase; lipid methyl transferase; phosphatidylethanolamine methyltransferase; phosphatidylethanolamine-N-methylase; phosphatidylethanolamine-S-adenosylmethionine methyltransferase
Systematic name: S-adenosyl-L-methionine:phosphatidylethanolamine N-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-91-0
References:
1. Hirata, F., Viveros, O.H., Diliberto, E.J., Jr. and Axelrod, J. Identification and properties of two methyltransferases in conversion of phosphatidylethanolamine to phosphatidylcholine. Proc. Natl. Acad. Sci. USA 75 (1978) 1718-1721. [PMID: 25437]
2. Morgan, T.E. Isolation and characterization of lipid N-methyltransferase from dog lung. Biochim. Biophys. Acta 178 (1969) 21-34. [PMID: 5773456]
3. Schneider, W.J. and Vance, D.E. Conversion of phosphatidylethanolamine to phosphatidylcholine in rat liver. Partial purification and characterization of the enzymatic activities. J. Biol. Chem. 254 (1979) 3886-3891. [PMID: 438165]
Accepted name: polysaccharide O-methyltransferase
Reaction: S-adenosyl-L-methionine + (1→4)-α-D-glucooligosaccharide = S-adenosyl-L-homocysteine + oligosaccharide containing 6-methyl-D-glucose units
Other name(s): polysaccharide methyltransferase; acylpolysacharide 6-methyltransferase; S-adenosyl-L-methionine:1,4-α-D-glucan 6-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:(1→4)-α-D-glucan 6-O-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37205-56-4
References:
1. Ferguson, J.A. and Ballou, C.E. Biosynthesis of a mycobacterial lipopolysaccharide. Properties of the polysaccharide methyltransferase. J. Biol. Chem. 245 (1970) 4213-4223. [PMID: 5503262]
Accepted name: trimethylsulfonium—tetrahydrofolate N-methyltransferase
Reaction: trimethylsulfonium + tetrahydrofolate = dimethylsulfide + 5-methyltetrahydrofolate
For diagram of reaction click here.
Other name(s): trimethylsulfonium-tetrahydrofolate methyltransferase
Systematic name: trimethylsulfonium:tetrahydrofolate N-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-92-1
References:
1. Wagner, C., Lusty, S.M., Jr., Kung, H.-F. and Rodgers, N.L. Preparation and properties of trimethylsulfonium-tetrahydrofolate methyltransferase. J. Biol. Chem. 242 (1967) 1287-1293. [PMID: 6023571]
Accepted name: glycine N-methyltransferase
Reaction: S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
Glossary: sarcosine = N-methylglycine
Other name(s): glycine methyltransferase; S-adenosyl-L-methionine:glycine methyltransferase; GNMT
Systematic name: S-adenosyl-L-methionine:glycine N-methyltransferase
Comments: This enzyme is thought to play an important role in the regulation of methyl group metabolism in the liver and pancreas by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. It is inhibited by 5-methyltetrahydrofolate pentaglutamate [4]. Sarcosine, which has no physiological role, is converted back into glycine by the action of EC 1.5.99.1, sarcosine dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37228-72-1
References:
1. Blumenstein, J. and Williams, G.R. Glycine methyltransferase. Can. J. Biochem. Physiol. 41 (1963) 201-210. [PMID: 13971907]
2. Ogawa, H., Gomi, T., Takusagawa, F. and Fujioka, M. Structure, function and physiological role of glycine N-methyltransferase. Int. J. Biochem. Cell Biol. 30 (1998) 13-26. [PMID: 9597750]
3. Yeo, E.J., Briggs, W.T. and Wagner, C. Inhibition of glycine N-methyltransferase by 5-methyltetrahydrofolate pentaglutamate. J. Biol. Chem. 274 (1999) 37559-37564. [PMID: 10608809]
4. Martinov, M.V., Vitvitsky, V.M., Mosharov, E.V., Banerjee, R. and Ataullakhanov, F.I. A substrate switch: a new mode of regulation in the methionine metabolic pathway. J. Theor. Biol. 204 (2000) 521-532. [PMID: 10833353]
5. Takata, Y., Huang, Y., Komoto, J., Yamada, T., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M. and Takusagawa, F. Catalytic mechanism of glycine N-methyltransferase. Biochemistry 42 (2003) 8394-8402. [PMID: 12859184]
6. Pakhomova, S., Luka, Z., Grohmann, S., Wagner, C. and Newcomer, M.E. Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes. Proteins 57 (2004) 331-337. [PMID: 15340920]
Accepted name: methylamine—glutamate N-methyltransferase
Reaction: methylamine + L-glutamate = NH3 + N-methyl-L-glutamate
Other name(s): N-methylglutamate synthase; methylamine-glutamate methyltransferase
Systematic name: methylamine:L-glutamate N-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9045-32-3
References:
1. Shaw, W.V., Tsai, L. and Stadtman, E.R. The enzymatic synthesis of N-methylglutamic acid. J. Biol. Chem. 241 (1966) 935-945. [PMID: 5905132]
Accepted name: carnosine N-methyltransferase
Reaction: S-adenosyl-L-methionine + carnosine = S-adenosyl-L-homocysteine + anserine
Systematic name: S-adenosyl-L-methionine:carnosine N-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-93-2
References:
1. McManus, I.R. Enzymatic synthesis of anserine in skeletal muscle by N-methylation of carnosine. J. Biol. Chem. 237 (1962) 1207-1211.
[EC 2.1.1.23 Deleted entry: protein-arginine N-methyltransferase. Now listed as EC 2.1.1.124 [cytochrome c]-arginine N-methyltransferase, EC 2.1.1.125 histone-arginine N-methyltransferase and EC 2.1.1.126 [myelin basic protein]-arginine N-methyltransferase. (EC 2.1.1.23 created 1972, modified 1976, modified 1983, deleted 1999)]
[EC 2.1.1.24 Deleted entry: protein-γ-glutamate O-methyltransferase. Now listed as EC 2.1.1.77 protein-L-isoaspartate(D-aspartate) O-methyltransferase, EC 2.1.1.80 protein-glutamate O-methyltransferase and EC 2.1.1.100 protein-S-isoprenylcysteine O-methyltransferase. (EC 2.1.1.24 created 1972, modified 1983, modified 1989, deleted 1992)]
Accepted name: phenol O-methyltransferase
Reaction: S-adenosyl-L-methionine + phenol = S-adenosyl-L-homocysteine + anisole
Other name(s): PMT
Systematic name: S-adenosyl-L-methionine:phenol O-methyltransferase
Comments: Acts on a wide variety of simple alkyl-, methoxy- and halo-phenols.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-94-3
References:
1. Axelrod, J. and Daly, J. Phenol-O-methyltransferase. Biochim. Biophys. Acta 159 (1968) 472-478. [PMID: 5657870]
Accepted name: iodophenol O-methyltransferase
Reaction: S-adenosyl-L-methionine + 2-iodophenol = S-adenosyl-L-homocysteine + 2-iodophenol methyl ether
Systematic name: S-adenosyl-L-methionine:2-iodophenol O-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-95-4
References:
1. Tomita, K., Cha, C.-J. and Lardy, H.A. Enzymic O-methylation of iodinated phenols and thyroid hormones. J. Biol. Chem. 239 (1964) 1202-1207.
Accepted name: tyramine N-methyltransferase
Reaction: S-adenosyl-L-methionine + tyramine = S-adenosyl-L-homocysteine + N-methyltyramine
Other name(s): DIB O-methyltransferase (3,5-diiodo-4-hydroxy-benzoic acid); S-adenosyl-methionine:tyramine N-methyltransferase; tyramine methylpherase
Systematic name: S-adenosyl-L-methionine:tyramine N-methyltransferase
Comments: Has some activity on phenylethylamine analogues.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-96-5
References:
1. Mann, J.D. and Mudd, S.H. Alkaloids and plant metabolism. IV. The tyramine methylpherase of barley roots. J. Biol. Chem. 238 (1963) 381-385.
Accepted name: phenylethanolamine N-methyltransferase
Reaction: S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine
For diagram click here.
Other name(s): noradrenaline N-methyltransferase; noradrenalin N-methyltransferase; norepinephrine methyltransferase; norepinephrine N-methyltransferase; phenethanolamine methyltransferase; phenethanolamine N-methyltransferase
Systematic name: S-adenosyl-L-methionine:phenylethanolamine N-methyltransferase
Comments: Acts on various phenylethanolamines; converts noradrenaline into adrenaline.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9037-68-7
References:
1. Axelrod, J. Purification and properties of phenylethanolamine-N-methyl transferase. J. Biol. Chem. 237 (1962) 1657-1660.
2. Connett, R.J. and Kirschner, N. Purification and properties of bovine phenylethanolamine N-methyltransferase. J. Biol. Chem. 245 (1970) 329-334. [PMID: 5412063]
Accepted name: tRNA (cytosine-5-)-methyltransferase
Reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 5-methylcytosine
Other name(s): transfer ribonucleate cytosine 5-methyltransferase; transfer RNA cytosine 5-methyltransferase
Systematic name: S-adenosyl-L-methionine:tRNA (cytosine-5-)-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37256-97-6
References:
1. Björk, G.R. and Svensson, I. Studies on microbial RNA. Fractionation of tRNA methylases from Saccharomyces cerevisiae. Eur. J. Biochem. 9 (1969) 207-215. [PMID: 4896260]
2. Hurwitz, J., Gold, M. and Anders, M. The enzymatic methylation of ribonucleic acid and deoxyribonucleic acid. 3. Purification of soluble ribonucleic acid-methylating enzymes. J. Biol. Chem. 239 (1964) 3462-3473.
3. Keith, J.M., Winters, E.M. and Moss, B. Purification and characterization of a HeLa cell transfer RNA(cytosine-5-)-methyltransferase. J. Biol. Chem. 255 (1980) 4636-4644. [PMID: 7372600]
[EC 2.1.1.30 Deleted entry: tRNA (purine-2- or -6-)-methyltransferase. Reactions previously described are due to EC 2.1.1.32 tRNA (guanine-N2-)-methyltransferase. (EC 2.1.1.30 created 1972, deleted 1981)]
Accepted name: tRNA (guanine-N1-)-methyltransferase
Reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine
Other name(s): transfer ribonucleate guanine 1-methyltransferase; tRNA guanine 1-methyltransferase
Systematic name: S-adenosyl-L-methionine:tRNA (guanine-N1-)-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37256-99-8
References:
1. Björk, G.R. and Svensson, I. Studies on microbial RNA. Fractionation of tRNA methylases from Saccharomyces cerevisiae. Eur. J. Biochem. 9 (1969) 207-215. [PMID: 4896260]
2. Glick, J.M., Averyhart, V.M. and Leboy, P.S. Purification and characterization of two tRNA-(guanine)-methyltransferases from rat liver. Biochim. Biophys. Acta 518 (1978) 158-171. [PMID: 629973]
3. Hurwitz, J., Gold, M. and Anders, M. The enzymatic methylation of ribonucleic acid and deoxyribonucleic acid. 3. Purification of soluble ribonucleic acid-methylating enzymes. J. Biol. Chem. 239 (1964) 3462-3473.
4. Smolar, N., Hellman, V. and Svennson, I. Two transfer RNA (1-methylguanine) methylases from yeast. Nucleic Acids Res. 2 (1975) 993-1004. [PMID: 1096087]
Accepted name: tRNA (guanine-N2-)-methyltransferase
Reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N2-methylguanine
Other name(s): transfer ribonucleate guanine 2-methyltransferase; transfer ribonucleate guanine N2-methyltransferase; transfer RNA guanine 2-methyltransferase; guanine-N2-methylase
Systematic name: S-adenosyl-L-methionine:tRNA (guanine-N2-)-methyltransferase
Comments: In eukaryotic tRNAs, two N2-guanine methylations occur, at the N2-methylguanine at position 10 and the N2-methylguanine at position 29.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37217-31-5, 60120-51-6
References:
1. Agris, P.F., Spremulli, L. and Brown, G.M. tRNA methylases from HeLa cells: purification and properties of an adenine-1-methylase and a guanine-N2-methylase. Arch. Biochem. Biophys. 162 (1974) 38-47. [PMID: 4208689]
2. Baguley, B.C. and Staehelin, M. The specificity of transfer ribonucleic acid methylases from rat liver. Biochemistry 7 (1968) 45-50. [PMID: 4921283]
3. Björk, G.R. and Svensson, I. Studies on microbial RNA. Fractionation of tRNA methylases from Saccharomyces cerevisiae. Eur. J. Biochem. 9 (1969) 207-215. [PMID: 4896260]
4. Glick, J.M., Averyhart, V.M. and Leboy, P.S. Purification and characterization of two tRNA-(guanine)-methyltransferases from rat liver. Biochim. Biophys. Acta 518 (1978) 158-171. [PMID: 629973]
5. Glick, J.M., Ross, S. and Leboy, P.S. S-Adenosylhomocysteine inhibition of three purified tRNA methyltransferases from rat liver. Nucleic Acids Res. 2 (1975) 1639-1651. [PMID: 1208211]
6. Izzo, P. and Gantt, R. Partial purification and characterization of an N2-guanine RNA methyltransferase from chicken embryos. Biochemistry 16 (1977) 3576-3581. [PMID: 19056]
7. Krauss, J. and Stahelin, M. N2-Guanine specific transfer RNA methyltransferase I from rat liver and leukemic rat spleen. Nucleic Acids Res. 1 (1974) 1455-1478.
8. Krauss, J. and Stahelin, M. N2-Guanine specific transfer RNA methyltransferase II from rat liver. Nucleic Acids Res. 1 (1974) 1479-1496.
Accepted name: tRNA (guanine-N7-)-methyltransferase
Reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine
Other name(s): transfer ribonucleate guanine 7-methyltransferase; 7-methylguanine transfer ribonucleate methylase; tRNA guanine 7-methyltransferase; N7-methylguanine methylase
Systematic name: S-adenosyl-L-methionine:tRNA (guanine-N7-)-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-00-4
References:
1. Aschhoff, H.J., Elten, H., Arnold, H.H., Mahal, G., Kersten, W. and Kersten, H. 7-Methylguanine specific tRNA-methyltransferase from Escherichia coli. Nucleic Acids Res. 3 (1976) 3109-3122. [PMID: 794833]
2. Björk, G.R. and Svensson, I. Studies on microbial RNA. Fractionation of tRNA methylases from Saccharomyces cerevisiae. Eur. J. Biochem. 9 (1969) 207-215. [PMID: 4896260]
3. Hurwitz, J., Gold, M. and Anders, M. The enzymatic methylation of ribonucleic acid and deoxyribonucleic acid. 3. Purification of soluble ribonucleic acid-methylating enzymes. J. Biol. Chem. 239 (1964) 3462-3473.
4. Salvatore, F., Traboni, C., Colonna, A., Ciliberto, G., Paoletta, C. and Cimino, F. In: Cavallini, D., Gaul, G.E. and Zappia, V. (Eds.), Natural Sulfur Compounds, Plenum Press, New York, 1980, p. 25.
Accepted name: tRNA guanosine-2'-O-methyltransferase
Reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanosine
Other name(s): transfer ribonucleate guanosine 2'-methyltransferase; tRNA guanosine 2'-methyltransferase; tRNA (guanosine 2')-methyltransferase; tRNA (Gm18) 2'-O-methyltransferase; tRNA (Gm18) methyltransferase; tRNA (guanosine-2'-O-)-methyltransferase; S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase
Systematic name: S-adenosyl-L-methionine:tRNA guanosine-2'-O-methyltransferase
Comments: Methylates the 2'-hydroxy group of a guanosine present in a GG sequence at position 18. Yeast tRNAPhe is one of the best substrate tRNAs.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37257-01-5
References:
1. Gefter, M.L. The in vitro synthesis of 2'-O-methylguanosine and 2-methylthio 6N (γγ-dimethylallyl) adenosine in transfer RNA of Escherichia coli. Biochem. Biophys. Res. Commun. 36 (1969) 435-441. [PMID: 4898378]
2. Kumagai, I., Watanabe, K. and Oshima, T. Thermally induced biosynthesis of 2'-O-methylguanosine in tRNA from an extreme thermophile, Thermus thermophilus HB27. Proc. Natl. Acad. Sci. USA 77 (1980) 1922-1926. [PMID: 6990416]
3. Hori, H., Yamazaki, N., Matsumoto, T., Watanabe, Y., Ueda, T., Nishikawa, K., Kumagai, I. and Watanabe, K. Substrate recognition of tRNA (guanosine-2'-)-methyltransferase from Thermus thermophilus HB27. J. Biol. Chem. 273 (1998) 25721-25727. [PMID: 9748240]
Accepted name: tRNA (uracil-5-)-methyltransferase
Reaction: S-adenosyl-L-methionine + tRNA containing uridine at position 54 = S-adenosyl-L-homocysteine + tRNA containing ribothymidine at position 54
Glossary: Ψ = pseudouridine
T = ribothymidine = 5-methyluridine
Other name(s): ribothymidyl synthase; transfer RNA uracil 5-methyltransferase; transfer RNA uracil methylase; tRNA uracil 5-methyltransferase; m5U-methyltransferase; tRNA:m5U54-methyltransferase; RUMT
Systematic name: S-adenosyl-L-methionine:tRNA (uracil-5-)-methyltransferase
Comments: Up to 25% of the bases in mature tRNA are post-translationally modified or hypermodified. One almost universal post-translational modification is the conversion of U54 (in the TΨC loop) into ribothymidine (5-methyluridine), and this modification is found in most species studied to date [7]. Unlike this enzyme, EC 2.1.1.74, methylenetetrahydrofolate—tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing), uses 5,10-methylenetetrahydrofolate and FADH2 to supply the atoms for methylation of U54[4].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-02-6
References:
1. Björk, G.R. and Svensson, I. Studies on microbial RNA. Fractionation of tRNA methylases from Saccharomyces cerevisiae. Eur. J. Biochem. 9 (1969) 207-215. [PMID: 69267419]
2. Greenberg, R. and Dudock, B. Isolation and characterization of m5U-methyltransferase from Escherichia coli. J. Biol. Chem. 255 (1980) 8296-8302. [PMID: 81006849]
3. Hurwitz, J., Gold, M. and Anders, M. The enzymatic methylation of ribonucleic acid and deoxyribonucleic acid. 3. Purification of soluble ribonucleic acid-methylating enzymes. J. Biol. Chem. 239 (1964) 3462-3473.
4. Delk, A.S., Nagle, D.P., Jr. and Rabinowitz, J.C. Methylenetetrahydrofolate-dependent biosynthesis of ribothymidine in transfer RNA of Streptococcus faecalis. Evidence for reduction of the 1-carbon unit by FADH2. J. Biol. Chem. 255 (1980) 4387-4390. [PMID: 6768721]
5. Kealey, J.T., Gu, X. and Santi, D.V. Enzymatic mechanism of tRNA (m5U54)methyltransferase. Biochimie 76 (1994) 1133-1142. [PMID: 7748948]
6. Gu, X., Ivanetich, K.M. and Santi, D.V. Recognition of the T-arm of tRNA by tRNA (m5U54)-methyltransferase is not sequence specific. Biochemistry 35 (1996) 11652-11659. [PMID: 8794745]
7. Becker, H.F., Motorin, Y., Sissler, M., Florentz, C. and Grosjean, H. Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the TΨ-loop of yeast tRNAs. J. Mol. Biol. 274 (1997) 505-518. [PMID: 9417931]
Accepted name: tRNA (adenine-N1-)-methyltransferase
Reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N1-methyladenine
Other name(s): transfer ribonucleate adenine 1-methyltransferase; transfer RNA (adenine-1) methyltransferase; 1-methyladenine transfer RNA methyltransferase; adenine-1-methylase
Systematic name: S-adenosyl-L-methionine:tRNA (adenine-N1-)-methyltransferase
Comments: The enzymes from different sources are specific for different adenine residues in tRNA.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-03-7
References:
1. Baguley, B.C. and Staehelin, M. The specificity of transfer ribonucleic acid methylases from rat liver. Biochemistry 7 (1968) 45-50. [PMID: 4921283]
2. Björk, G.R. and Svensson, I. Studies on microbial RNA. Fractionation of tRNA methylases from Saccharomyces cerevisiae. Eur. J. Biochem. 9 (1969) 207-215. [PMID: 4896260]
3. Dubois, E.E., Dirheimer, G. and Weil, J.H. Methylation of yeast tRNA Asp by enzymes from cytoplasm, chloroplasts and mitochondria of Phaseolus vulgaris. Biochim. Biophys. Acta 374 (1974) 332-341. [PMID: 4611497]
4. Glick, J.M. and Leboy, P.S. Purification and properties of tRNA(adenine-1)-methyltransferase from rat liver. J. Biol. Chem. 252 (1977) 4790-4795. [PMID: 17605]
Accepted name: DNA (cytosine-5-)-methyltransferase
Reaction: S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
Other name(s): EcoRI methylase; DNA 5-cytosine methylase; DNA cytosine c5 methylase; DNA cytosine methylase; DNA methylase; DNA methyltransferase; DNA transmethylase; DNA-cytosine 5-methylase; DNA-cytosine methyltransferase; HpaII methylase; HpaII' methylase; M.BsuRIa; M.BsuRIb; Type II DNA methylase; cytosine 5-methyltransferase; cytosine DNA methylase; cytosine DNA methyltransferase; cytosine-specific DNA methyltransferase; deoxyribonucleate methylase; deoxyribonucleate methyltransferase; deoxyribonucleic (cytosine-5-)-methyltransferase; deoxyribonucleic acid (cytosine-5-)-methyltransferase; deoxyribonucleic acid methylase; deoxyribonucleic acid methyltransferase; deoxyribonucleic acid modification methylase; deoxyribonucleic methylase; methylphosphotriester-DNA methyltransferase; modification methylase; restriction-modification system; site-specific DNA-methyltransferase (cytosine-specific)
Systematic name: S-adenosyl-L-methionine:DNA (cytosine-5-)-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9037-42-7
References:
1. Gold, M. and Hurwitz, J. The enzymatic methylation of ribonucleic acid and deoxyribonucleic acid. V. Purification and properties of the deoxyribonucleic acid-methylating activity of Escherichia coli. J. Biol. Chem. 239 (1964) 3858-2865.
2. Kalousek, F. and Morris, N.R. The purification and properties of deoxyribonucleic acid methylase from rat spleen. J. Biol. Chem. 244 (1969) 1157-1163. [PMID: 4975067]
3. Roy, P.H. and Weissbach, A. DNA methylase from HeLa cell nuclei. Nucleic Acids Res. 2 (1975) 1669-1684. [PMID: 1187340]
4. Simon, D., Grunert, F., Acken, U.Y., Döring, H.P. and Kröger, H. DNA-methylase from regenerating rat liver: purification and characterisation. Nucleic Acids Res. 5 (1978) 2153-2167. [PMID: 673848]
5. Sneider, T.W., Teague, W.M. and Rogachewsky, L.M. S-Adenosylmethionine: DNA-cytosine 5-methyltransferase from a Novikoff rat hepatoma cell line. Nucleic Acids Res. 2 (1975) 1685-1700. [PMID: 171625]
6. Turnbull, J.F. and Adams, R.L.P. DNA methylase: purification from ascites cells and the effect of various DNA substrates on its activity. Nucleic Acids Res. 3 (1976) 677-695. [PMID: 131936]
7. Kessler, C. and Manta, V. Specificity of restriction endonucleases and DNA modification methyltransferases: a review. Gene 92 (1990) 1-248. [PMID: 91032997]
8. Roberts, R.J. Restriction enzymes and their isoschizomers. Nucleic Acids Res. 18 (1990) 2331-2365. [PMID: 2159140]
9. Yuan, R. Structure and mechanism of multifunctional restriction endonucleases. Annu. Rev. Biochem. 50 (1981) 285-319. [PMID: 6267988]
Accepted name: O-demethylpuromycin O-methyltransferase
Reaction: S-adenosyl-L-methionine + O-demethylpuromycin = S-adenosyl-L-homocysteine + puromycin
Other name(s): O-demethylpuromycin methyltransferase
Systematic name: S-adenosyl-L-methionine:O-demethylpuromycin O-methyltransferase
Comments: Puromycin is the antibiotic derived from N6-dimethyladenosine by replacing the 3'-hydroxy group with an amino group and acylating this with 4-O-methyltyrosine.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-04-8
References:
1. Rao, M.M., Rebello, P.F. and Pogell, B.M. Biosynthesis of puromycin in Streptomyces alboniger. Enzymatic methylation of O-demethylpuromycin. J. Biol. Chem. 244 (1969) 112-118. [PMID: 5773275]
Accepted name: inositol 3-methyltransferase
Reaction: S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-3-O-methyl-myo-inositol
For diagram click here.
Other name(s): inositol L-1-methyltransferase; myo-inositol 1-methyltransferase; S-adenosylmethionine:myo-inositol 1-methyltransferase; myo-inositol 1-O-methyltransferase (name based on 1L-numbering system and not 1D-numbering); S-adenosyl-L-methionine:myo-inositol 1-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:1D-myo-inositol 3-O-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-05-9
References:
1. Hofmann, H., Wagner, I. and Hoffmann-Ostenhof, O. Untersuchungen über die Biosynthese der Cyclite. XXIV. Über ein lösliches Enzym aus Vinca rosea, das myo-Inosit zu L-Bornesit methyliert. Hoppe-Seyler's Z. Physiol. Chem. 350 (1969) 1465-1468. [PMID: 5362621]
Accepted name: inositol 1-methyltransferase
Reaction: S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-1-O-methyl-myo-inositol
For diagram click here.
Other name(s): inositol D-1-methyltransferase; S-adenosylmethionine:myo-inositol 3-methyltransferase; myo-inositol 3-O-methyltransferase; inositol 3-O-methyltransferase (name based on 1L-numbering system and not 1D-numbering); S-adenosyl-L-methionine:myo-inositol 3-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:1D-myo-inositol 1-O-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-06-0
References:
1 .Wagner, I., Hofmann, H. and Hoffmann-Ostenhof, O. Untersuchungen über die Biosynthese der Cyclite. XXIII. Über ein lösliches Enzym aus Erbsenkeimlingen, das myo-Inosit zu D-Bornesit methyliert. Hoppe-Seyler's Z. Physiol. Chem. 350 (1969) 1460-1464. [PMID: 5362620]
Accepted name: sterol 24-C-methyltransferase
Reaction: S-adenosyl-L-methionine + 5α-cholesta-8,24-dien-3β-ol = S-adenosyl-L-homocysteine + 24-methylene-5α-cholest-8-en-3β-ol
For diagram click here.
Glossary entries:
desmosterol = cholesta-5,24-dien-3β-ol
zymostrol = 5α-cholesta-8,24-dien-3β-ol
Other name(s): δ24-methyltransferase; δ24-sterol methyltransferase; zymosterol-24-methyltransferase; S-adenosyl-4-methionine:sterol δ24-methyltransferase; SMT1; 24-sterol C-methyltransferase; S-adenosyl-L-methionine:δ24(23)-sterol methyltransferase; phytosterol methyltransferase
Systematic name: S-adenosyl-L-methionine:zymosterol 24-C-methyltransferase
Comments: Requires glutathione. Acts on a range of sterols with a 24(25)-double bond in the sidechain. While zymosterol is the preferred substrate it also acts on desmosterol, 5α-cholesta-7,24-dien-3β-ol, 5α-cholesta-5,7,24-trien-3β-ol, 4α-methylzymosterol and others. S-Adenosyl-L-methionine attacks the Si-face of the 24(25) double bond and the C-24 hydrogen is transferred to C-25 on the Re face of the double bond.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37257-07-1
References:
1. Moore, J.T., Jr. and Gaylor, J.L. Isolation and purification of an S-adenosylmethionine: δ24-sterol methyltransferase from yeast. J. Biol. Chem. 244 (1969) 6334-6340. [PMID: 5354959]
2. Venkatramesh, M., Guo, D., Jia, Z. and Nes, W.D. Mechanism and structural requirements for transformations of substrates by the S-adenosyl-L-methionine:δ24(25)-sterol methyl transferase enzyme from Saccharomyces cerevisiae. Biochim. Biophys. Acta 1299 (1996) 313-324. [PMID: 8597586]
3. Tong, Y., McCourt, B.S., Guo, D., Mangla, A.T., Zhou, W.X., Jenkins, M.D., Zhou, W., Lopez, M. and Nes, W.D., Stereochemical features of C-methylation on the path to δ24(28)-methylene and δ24(28)-ethylidene sterols: studies on the recombinant phytosterol methyl transferase from Arabidopsis thaliana. Tetrahedron Lett. 38 (1997) 6115-6118.
4. Bouvier-Navé, P., Husselstein, T. and Benveniste, P. Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant biosynthesis. Eur. J. Biochem. 256 (1998) 88-96. [PMID: 9746350]
5. Nes, W.D., McCourt, B.S., Zhou, W., Ma, J., Marshall, J.A., Peek, L.A. and Brennan, M. Overexpression, purification, and stereochemical studies of the recombinant S-adenosyl-L-methionine:δ24(25)- to δ24(28)-sterol methyl transferase enzyme from Saccharomyces cerevisiae sterol methyl transferase. Arch. Biochem. Biophys. 353 (1998) 297-311. [PMID: 9606964]
Accepted name: luteolin O-methyltransferase
Reaction: S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone = S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone
For diagram click here.
See diagram for reaction in biochanin A or formononetin biosynthesis.
Other name(s): o-dihydric phenol methyltransferase; luteolin methyltransferase; luteolin 3'-O-methyltransferase; o-diphenol m-O-methyltransferase; o-dihydric phenol meta-O-methyltransferase; S-adenosylmethionine:flavone/flavonol 3'-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:5,7,3',4'-tetrahydroxyflavone 3'-O-methyltransferase
Comments: Also acts on luteolin 7-O-β-D-glucoside.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37205-55-3
References:
1. Ebel, J., Hahlbrock, K. and Grisebach, H. Purification and properties of an o-dihydricphenol meta-O-methyltransferase from cell suspension cultures of parsley and its relation to flavonoid biosynthesis. Biochim. Biophys. Acta 268 (1972) 313-326. [PMID: 5026305]
Accepted name: histone-lysine N-methyltransferase
Reaction: S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
Other name(s): protein methylase III; protein methylase 3; protein (lysine) methyltransferase; protein methyltransferase II; protein-lysine N-methyltransferase; histone H1-specific S-adenosylmethionine:protein-lysine N-methyltransferase
Systematic name: S-adenosyl-L-methionine:histone-L-lysine N6-methyltransferase
Comments: One of a group of enzymes methylating proteins; see also EC 2.1.1.59 [cytochrome-c]-lysine N-methyltransferase and EC 2.1.1.60 calmodulin-lysine N-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9055-08-7
References:
1. Paik, W.K. and Kim, S. Solubilization and partial purification of protein methylase 3 from calf thymus nuclei. J. Biol. Chem. 245 (1970) 6010-6015. [PMID: 5484460]
2. Venkatesan, M. and McManus, I.R. Partial purification and characterization of a protein lysine methyltransferase from plasmodia of Physarum polycephalum. Biochemistry 18 (1979) 5365-5371. [PMID: 391266]
Accepted name: dimethylhistidine N-methyltransferase
Reaction: S-adenosyl-L-methionine + Nα,Nα-dimethyl-L-histidine = S-adenosyl-L-homocysteine + Nα,Nα,Nα-trimethyl-L-histidine
Other name(s): dimethylhistidine methyltransferase; histidine-α-N-methyltransferase
Systematic name: S-adenosyl-L-methionine:Nα,Nα-dimethyl-L-histidine Nα-methyltransferase
Comments: Methylhistidine and histidine can also act as methyl acceptors, with trimethylhistidine being formed in both cases.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 62213-53-0
References:
1. Ishikawa, Y. and Melville, D.B. The enzymatic α-N-methylation of histidine. J. Biol. Chem. 245 (1970) 5967-5973. [PMID: 5484456]
Accepted name: thymidylate synthase
Reaction: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
For diagram of reaction click here.
Other name(s): dTMP synthase; thymidylate synthetase; methylenetetrahydrofolate:dUMP C-methyltransferase; TMP synthetase
Systematic name: 5,10-methylenetetrahydrofolate:dUMP C-methyltransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, CAS registry number: 9031-61-2
References:
1. Blakley, R.L. The biosynthesis of thymidylic acid. IV. Further studies on thymidylate synthase. J. Biol. Chem. 238 (1963) 2113-2118.
2. Lockshin, A., Moran, R.G. and Danenberg, P.V. Thymidylate synthetase purified to homogeneity from human leukemic cells. Proc. Natl. Acad. Sci. USA 76 (1979) 750-754. [PMID: 34155]
3. Slavik, K. and Slavikova, V. Purification of thymidylate synthetase from enzyme-poor sources by affinity chromatography. Methods Enzymol. 66 (1980) 709-723. [PMID: 6990200]
4. Wahba, A.J. and Friedkin, M. The enzymatic synthesis of thymidylate. I. Early steps in the purification of thymidylate synthetase of Escherichia coli. J. Biol. Chem. 237 (1962) 3794-3801.
Accepted name: isoflavone 4'-O-methyltransferase
Reaction: S-adenosyl-L-methionine + an isoflavone = S-adenosyl-L-homocysteine + a 4'-O-methylisoflavone
See diagram for reaction in biochanin A or formononetin biosynthesis.
Other name(s): 4'-hydroxyisoflavone methyltransferase; isoflavone methyltransferase; isoflavone O-methyltransferase
Systematic name: S-adenosyl-L-methionine:isoflavone 4'-O-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 55071-80-2
References:
1. Wengenmayer, H., Ebel, J. and Grisebach, H. Purification and properties of a S-adenosylmethionine: isoflavone 4'-O-methyltransferase from cell suspension cultures of Cicer arietinum L. Eur. J. Biochem. 50 (1974) 135-143. [PMID: 4452353]
Accepted name: indolepyruvate C-methyltransferase
Reaction: S-adenosyl-L-methionine + (indol-3-yl)pyruvate = S-adenosyl-L-homocysteine + (S)-3-(indol-3-yl)-2-oxobutanoate
Other name(s): indolepyruvate methyltransferase; indolepyruvate 3-methyltransferase; indolepyruvic acid methyltransferase; S-adenosyl-L-methionine:indolepyruvate C-methyltransferase
Systematic name: S-adenosyl-L-methionine:(indol-3-yl)pyruvate C-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 54576-88-4
References:
1. Hornemann, U., Speedie, M.K., Hurley, L.H. and Floss, H.G. Demonstration of a C-methylating enzyme in cell free extracts of indolmycin-producing Streptomyces griseus. Biochem. Biophys. Res. Commun. 39 (1970) 594-599. [PMID: 5490210]
Accepted name: rRNA (adenine-N6-)-methyltransferase
Reaction: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing N6-methyladenine
Other name(s): ribosomal ribonucleate adenine 6-methyltransferase; gene ksgA methyltransferase; ribonucleic acid-adenine (N6) methylase; ErmC 23S rRNA methyltransferase
Systematic name: S-adenosyl-L-methionine:rRNA (adenine-N6-)-methyltransferase
Comments: Also methylates 2-aminoadenosine to 2-methylaminoadenosine.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9076-81-7
References:
1. Sipe, J.E., Anderson, W.M., Jr., Remy, C.N. and Love, S.H. Characterization of S-adenosylmethionine: ribosomal ribonucleic acid-adenine (N6)-methyltransferase of Escherichia coli strain B. J. Bacteriol. 110 (1972) 81-91. [PMID: 4622906]
Accepted name: amine N-methyltransferase
Reaction: S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine
Other name(s): nicotine N-methyltransferase; tryptamine N-methyltransferase; arylamine N-methyltransferase; tryptamine methyltransferase
Systematic name: S-adenosyl-L-methionine:amine N-methyltransferase
Comments: An enzyme of very broad specificity; many primary, secondary and tertiary amines can act as acceptors, including tryptamine, aniline, nicotine and a variety of drugs and other xenobiotics.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 51377-47-0, 111694-10-1
References:
1. Ansher, S.S. and Jakoby, W.B. Amine N-methyltransferases from rabbit liver. J. Biol. Chem. 261 (1986) 3996-4001. [PMID: 3949799]
2. Crooks, P.A., Godin, C.S., Damani, L.A., Ansher, S.S. and Jakoby, W.B. Formation of quaternary amines by N-methylation of azaheterocycles with homogeneous amine N-methyltransferases. Biochem. Pharmacol. 37 (1988) 1673-1677. [PMID: 3377829]
Accepted name: loganate O-methyltransferase
Reaction: S-adenosyl-L-methionine + loganate = S-adenosyl-L-homocysteine + loganin
For diagram click here.
Other name(s): loganate methyltransferase; S-adenosyl-L-methionine:loganic acid methyltransferase
Systematic name: S-adenosyl-L-methionine:loganate 11-O-methyltransferase
Comments: Also acts on secologanate. Methylates the 11-carboxy group of the monoterpenoid loganate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 39391-10-1
References:
1. Madyastha, K.M., Guarnaccia, R., Baxter, C. and Coscia, C.J. S-Adenosyl-L-methionine: loganic acid methyltransferase. A carboxyl-alkylating enzyme from Vinca rosea. J. Biol. Chem. 248 (1973) 2497-2501. [PMID: 4698228]