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trans-aconitate 2-methyltransferase
trans-aconitate 2-methyltransferase
Identifiers
EC no.	2.1.1.144
CAS no.	235107-12-7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

In enzymology, a trans-aconitate 2-methyltransferase (EC 2.1.1.144) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + trans-aconitate

\rightleftharpoons

S-adenosyl-L-homocysteine + (E)-3-(methoxycarbonyl)pent-2-enedioate

Thus, the two substrates of this enzyme are S-adenosyl methionine and trans-aconitate, whereas its two products are S-adenosylhomocysteine and (E)-3-(methoxycarbonyl)pent-2-enedioate.

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 2'-O-methyltransferase.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2P35.

References

Cai H, Clarke S (1999). "A novel methyltransferase catalyzes the methyl esterification of trans-aconitate in Escherichia coli". J. Biol. Chem. 274 (19): 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 (7): 2210–9. doi:10.1021/bi0022902. PMID 11329290.
Cai H, Dumlao D, Katz JE, Clarke S (2001). "Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae". Biochemistry. 40 (45): 13699–709. doi:10.1021/bi011380j. PMID 11695919.