Trans-aconitate 3-methyltransferase

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In enzymology, a trans-aconitate 3-methyltransferase (EC 2.1.1.145) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + trans-aconitate $\rightleftharpoons$ S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate

Thus, the two substrates of this enzyme are S-adenosyl methionine and trans-aconitate, whereas its two products are S-adenosylhomocysteine and (E)-2-(methoxycarbonylmethyl)butenedioate.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 3'-O-methyltransferase.

[edit] References

IUBMB entry for 2.1.1.145
BRENDA references for 2.1.1.145 (Recommended.)
PubMed references for 2.1.1.145
PubMed Central references for 2.1.1.145
Google Scholar references for 2.1.1.145
Cai H, Clarke S (1999). "A novel methyltransferase catalyzes the methyl esterification of trans-aconitate in Escherichia coli". J. Biol. Chem. 274: 13470–9. doi:10.1074/jbc.274.19.13470. PMID 10224113.
Cai H, Strouse J, Dumlao D, Jung ME, Clarke S (2001). "Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferases". Biochemistry. 40: 2210–9. doi:10.1021/bi0022902. PMID 11329290.