| EC |
2.1.1.145 |
| Accepted name: |
trans-aconitate 3-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate |
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For diagram of reaction, click here |
| Glossary: |
trans-aconitate = (E)-prop-1-ene-1,2,3-tricarboxylate |
| Systematic name: |
S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 3′-O-methyltransferase |
| Comments: |
Also catalyses the formation of the methyl monoester of cis-aconitate, isocitrate and citrate, but more slowly. While the enzyme from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate as the product, that from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.144, trans-aconitate 2-methyltransferase) |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 235107-12-7 |
| References: |
| 1. |
Cai, H. and Clarke, S. A novel methyltransferase catalyzes the esterification of trans-aconitate in Escherichia coli. J. Biol. Chem. 274 (1999) 13470–13479. [DOI] [PMID: 10224113] |
| 2. |
Cai, H., Strouse, J., Dumlao, D., Jung, M.E. and Clarke, S. Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferase. Biochemistry 40 (2001) 2210–2219. [DOI] [PMID: 11329290] |
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| [EC 2.1.1.145 created 2002] |
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