ExplorEnz: EC 2.1.1.9*

Your query returned 11 entries. Printable version

2.1.1.9

Accepted name:

thiol S-methyltransferase

Reaction:

S-adenosyl-L-methionine + a thiol = S-adenosyl-L-homocysteine + a methyl 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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, 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. [DOI] [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. [DOI] [PMID: 485170]

[EC 2.1.1.9 created 1965]

2.1.1.90

Accepted name:

methanol—corrinoid protein Co-methyltransferase

Reaction:

methanol + a [Co(I) methanol-specific corrinoid protein] = a [methyl-Co(III) methanol-specific corrinoid protein] + H₂O

Other name(s):

methanol cobalamin methyltransferase; methanol:5-hydroxybenzimidazolylcobamide methyltransferase; MT 1 (ambiguous); methanol—5-hydroxybenzimidazolylcobamide Co-methyltransferase; mtaB (gene name)

Systematic name:

methanol:5-hydroxybenzimidazolylcobamide Co-methyltransferase

Comments:

The enzyme, which catalyses the transfer of methyl groups from methanol to a methanol-specific corrinoid protein (MtaC), is involved in methanogenesis from methanol. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. Free cob(I)alamin can substitute for the corrinoid protein in vitro [2]. Inactivated by oxygen and other oxidizing agents, and reactivated by catalytic amounts of ATP and hydrogen.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 86611-98-5

References:

1.	van der Meijden, P., te Brömmelstroet, B.W., Poirot, C.M., van der Drift, C. and Vogels, G.D. Purification and properties of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri. J. Bacteriol. 160 (1984) 629–635. [PMID: 6438059]
2.	Sauer, K. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri – substitution of the corrinoid harbouring subunit MtaC by free cob(I)alamin. Eur. J. Biochem. 261 (1999) 674–681. [DOI] [PMID: 10215883]

[EC 2.1.1.90 created 1989, modified 2012]

2.1.1.91

Accepted name:

isobutyraldoxime O-methyltransferase

Reaction:

S-adenosyl-L-methionine + 2-methylpropanal oxime = S-adenosyl-L-homocysteine + 2-methylpropanal O-methyloxime

Other name(s):

aldoxime methyltransferase; S-adenosylmethionine:aldoxime O-methyltransferase; aldoxime O-methyltransferase

Systematic name:

S-adenosyl-L-methionine:2-methylpropanal-oxime O-methyltransferase

Comments:

Oximes of C₄ to C₆ aldehydes can act as acceptors; the most active substrate is 2-methylbutyroaldoxime.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 95471-32-2

References:

1.	Harper, D.B. and Kennedy, J.T. Purification and properties of S-adenosylmethionine: aldoxime O-methyltransferase from Pseudomonas sp. N.C.I.B. 11652. Biochem. J. 226 (1985) 147–153. [PMID: 3977861]

[EC 2.1.1.91 created 1989]

2.1.1.92

Deleted entry:

bergaptol O-methyltransferase. Now included with EC 2.1.1.69, 5-hydroxyfuranocoumarin 5-O-methyltransferase. The reaction with bergaptol is a specific example of the general reaction associated with EC 2.1.1.69

[EC 2.1.1.92 created 1989, deleted 2006]

2.1.1.93

Deleted entry:

xanthotoxol O-methyltransferase. Enzyme is identical to EC 2.1.1.70, 8-hydroxyfuranocoumarin 8-O-methyltransferase

[EC 2.1.1.93 created 1989, deleted 2008]

2.1.1.94

Accepted name:

tabersonine 16-O-methyltransferase

Reaction:

S-adenosyl-L-methionine + 16-hydroxytabersonine = S-adenosyl-L-homocysteine + 16-methoxytabersonine

For diagram of vindoline biosynthesis, click here

Other name(s):

11-demethyl-17-deacetylvindoline 11-methyltransferase; 11-O-demethyl-17-O-deacetylvindoline O-methyltransferase; S-adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline 11-O-methyltransferase

Systematic name:

S-adenosyl-L-methionine:16-hydroxytabersonine 16-O-methyltransferase

Comments:

Involved in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle, Catharanthus roseus.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 100984-95-0

References:

1.	De Luca, V., Balsevich, J., Tyler, R.T., Eilert, U., Panchuk, B.D. and Kurz, W.G.W. Biosynthesis of indole alkaloids - developmental regulation of the biosynthetic-pathway from tabersonine to vindoline in Catharanthus roseus. J. Plant Physiol. 125 (1986) 147–156.
2.	Fahn, W., Laussermair, E., Deus-Neumann, B. and Stöckigt, J. Late enzymes of vindoline biosynthesis. S-Adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline 11-O-methylase and unspecific acetylesterase. Plant Cell Rep. 4 (1985) 337–340. [PMID: 24254077]

[EC 2.1.1.94 created 1989, modified 2005]

2.1.1.95

Accepted name:

tocopherol C-methyltransferase

Reaction:

(1) S-adenosyl-L-methionine + γ-tocopherol = S-adenosyl-L-homocysteine + α-tocopherol
(2) S-adenosyl-L-methionine + δ-tocopherol = S-adenosyl-L-homocysteine + β-tocopherol
(3) S-adenosyl-L-methionine + γ-tocotrienol = S-adenosyl-L-homocysteine + α-tocotrienol
(4) S-adenosyl-L-methionine + δ-tocotrienol = S-adenosyl-L-homocysteine + β-tocotrienol

For diagram of tocopherol biosynthesis, click here and for diagram of tocotrienol biosynthesis, click here

Other name(s):

γ-tocopherol methyltransferase; VTE4 (gene name); S-adenosyl-L-methionine:γ-tocopherol 5-O-methyltransferase (incorrect); tocopherol O-methyltransferase (incorrect)

Systematic name:

S-adenosyl-L-methionine:γ-tocopherol 5-C-methyltransferase

Comments:

The enzymes from plants and photosynthetic bacteria have similar efficiency with the γ and δ isomers of tocopherols and tocotrienols.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 84788-82-9

References:

1.	Camara, B. and d'Harlingue, A. Demonstration and solubilization of S-adenosylmethionine: γ-tocopherol methyltransferase from Capsicum chromoplasts. Plant Cell Rep. 4 (1985) 31–32. [DOI] [PMID: 24253640]
2.	Koch, M., Lemke, R., Heise, K.P. and Mock, H.P. Characterization of γ-tocopherol methyltransferases from Capsicum annuum L and Arabidopsis thaliana. Eur. J. Biochem. 270 (2003) 84–92. [DOI] [PMID: 12492478]
3.	Zhang, G.Y., Liu, R.R., Xu, G., Zhang, P., Li, Y., Tang, K.X., Liang, G.H. and Liu, Q.Q. Increased α-tocotrienol content in seeds of transgenic rice overexpressing Arabidopsis γ-tocopherol methyltransferase. Transgenic Res. 22 (2013) 89–99. [DOI] [PMID: 22763462]

[EC 2.1.1.95 created 1989, modified 2013, modified 2019]

2.1.1.96

Accepted name:

thioether S-methyltransferase

Reaction:

S-adenosyl-L-methionine + dimethyl sulfide = S-adenosyl-L-homocysteine + trimethylsulfonium

For diagram of dimethyl sulfide catabolism, click here

Other name(s):

S-adenosyl-L-methionine:thioether S-methyltransferase; thioether methyltransferase

Systematic name:

S-adenosyl-L-methionine:dimethyl-sulfide S-methyltransferase

Comments:

Also acts on dimethyl selenide, dimethyl telluride, diethyl sulfide, 1,4-dithiane and many other thioethers.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 114797-02-3

References:

1.	Mozier, N.M., McConnell, P. and Hoffman, J.L. S-Adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism. J. Biol. Chem. 263 (1988) 4527–4531. [PMID: 3350800]

[EC 2.1.1.96 created 1990]

2.1.1.97

Accepted name:

3-hydroxyanthranilate 4-C-methyltransferase

Reaction:

S-adenosyl-L-methionine + 3-hydroxyanthranilate = S-adenosyl-L-homocysteine + 3-hydroxy-4-methylanthranilate

Other name(s):

3-hydroxyanthranilate 4-methyltransferase

Systematic name:

S-adenosyl-L-methionine:3-hydroxyanthranilate 4-C-methyltransferase

Comments:

Involved in the biosynthesis of the antibiotic actinomycin in Streptomyces antibioticus.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 112445-22-4

References:

1.	Fawaz, F. and Jones, G.H. Actinomycin synthesis in Streptomyces antibioticus. Purification and properties of a 3-hydroxyanthranilate 4-methyltransferase. J. Biol. Chem. 263 (1988) 4602–4606. [PMID: 2450873]

[EC 2.1.1.97 created 1990]

2.1.1.98

Accepted name:

diphthine synthase

Reaction:

3 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] = 3 S-adenosyl-L-homocysteine + diphthine-[translation elongation factor 2] (overall reaction)
(1a) S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] = S-adenosyl-L-homocysteine + 2-[(3S)-3-carboxy-3-(methylamino)propyl]-L-histidine-[translation elongation factor 2]
(1b) S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-(methylamino)propyl]-L-histidine-[translation elongation factor 2] = S-adenosyl-L-homocysteine + 2-[(3S)-3-carboxy-3-(dimethylamino)propyl]-L-histidine-[translation elongation factor 2]
(1c) S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-(dimethylamino)propyl]-L-histidine-[translation elongation factor 2] = S-adenosyl-L-homocysteine + diphthine-[translation elongation factor 2]

For diagram of diphthamide biosynthesis, click here

Glossary:

diphthine = 2-[(3S)-3-carboxy-3-(trimethylamino)propyl]-L-histidine

Other name(s):

S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); S-adenosyl-L-methionine:2-(3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] methyltransferase; Dph5 (ambiguous)

Systematic name:

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

Comments:

This archaeal enzyme produces the trimethylated product diphthine, which is converted into diphthamide by EC 6.3.1.14, diphthine—ammonia ligase. Different from the eukaryotic enzyme, which produces diphthine methyl ester (cf. EC 2.1.1.314). In the archaeon Pyrococcus horikoshii the enzyme acts on His⁶⁰⁰ of elongation factor 2.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 114514-25-9

References:

1.	Zhu, X., Kim, J., Su, X. and Lin, H. Reconstitution of diphthine synthase activity in vitro. Biochemistry 49 (2010) 9649–9657. [DOI] [PMID: 20873788]

[EC 2.1.1.98 created 1990, modified 2013, modified 2015]

2.1.1.99

Accepted name:

3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase

Reaction:

S-adenosyl-L-methionine + 3-hydroxy-16-methoxy-2,3-dihydrotabersonine = S-adenosyl-L-homocysteine + deacetoxyvindoline

For diagram of vindoline biosynthesis, click here

Other name(s):

16-methoxy-2,3-dihydro-3-hydroxytabersonine methyltransferase; NMT; 16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase; S-adenosyl-L-methionine:16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase

Systematic name:

S-adenosyl-L-methionine:3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase

Comments:

Involved in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle Catharanthus roseus.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113478-40-3

References:

1.	De Luca, V., Balsevich, J., Tyler, R.T., Eilert, U., Panchuk, B.D. and Kurz, W.G.W. Biosynthesis of indole alkaloids - developmental regulation of the biosynthetic-pathway from tabersonine to vindoline in Catharanthus roseus. J. Plant Physiol. 125 (1986) 147–156.
2.	De Luca, V. and Cutler, A.J. Subcellular localization of enzymes involved in indole alkaloid biosynthesis in Catharanthus roseus. Plant Physiol. 85 (1987) 1099–1102. [PMID: 16665811]

[EC 2.1.1.99 created 1990, modified 2005]