| Entry |
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| Name |
trans-aconitate 3-methyltransferase
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| Class |
Transferases;
Transferring one-carbon groups;
Methyltransferases
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| Sysname |
S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 3'-O-methyltransferase
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| Reaction(IUBMB) |
S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate [RN: R05764]
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| Reaction(KEGG) |
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| Substrate |
S-adenosyl-L-methionine [CPD: C00019];
trans-aconitate [CPD: C02341]
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| Product |
S-adenosyl-L-homocysteine [CPD: C00021];
(E)-2-(methoxycarbonylmethyl)butenedioate [CPD: C11515]
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| Comment |
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)
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| History |
EC 2.1.1.145 created 2002
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| Orthology |
| K22438 | trans-aconitate 3-methyltransferase |
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| Genes |
» show all
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| Reference |
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| Authors |
Cai H, Clarke S. |
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| Title |
A novel methyltransferase catalyzes the methyl esterification of trans-aconitate in Escherichia coli. |
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| Journal |
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| Reference |
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| Authors |
Cai H, Strouse J, Dumlao D, Jung ME, Clarke S. |
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| Title |
Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferases. |
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| Journal |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 2.1.1.145 |
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