trans-aconitate 3-methyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.1.1.145 | ||||||||
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 | ||||||||
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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 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.
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.
Transferase: one carbon transferases (EC 2.1) | |||||||||
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2.1.1: Methyl- |
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2.1.2: Hydroxymethyl-, Formyl- and Related |
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2.1.3: Carboxy- and Carbamoyl |
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2.1.4: Amidine |
Enzymes | |
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