In enzymology, a trans-aconitate 2-methyltransferase (EC 2.1.1.144) is an enzyme that catalyzes the chemical reaction
| 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 | ||||||||
| |||||||||
- S-adenosyl-L-methionine + trans-aconitate 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
editAs of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2P35.
References
edit- 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.
