Trans-aconitate 2-methyltransferase
| Trans-aconitate 2-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.144 | ||||||||
| CAS no. | 235107-12-7 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Trans-aconitate 2-methyltransferase (EC 2.1.1.144) is an enzyme that catalyzes the chemical reaction
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-3-(methoxycarbonyl)pent-2-enedioic_acid.svg.png)
This is a methylation reaction in which trans-aconitic acid is converted to a mono-ester, trans-3-(methoxycarbonyl)pent-2-enedioic acid. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). The enzyme was characterised from Escherichia coli.[1][2][3]
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.[4]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 2P35.
See also
- Trans-aconitate 3-methyltransferase which converts the starting material into an alternative product.[3][4]
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.
- 1 2 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.
- 1 2 Enzyme 2.1.1.144 at KEGG Pathway Database.
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