2-pyrone-4,6-dicarboxylate lactonase

From Wikipedia, the free encyclopedia

In enzymology, a 2-pyrone-4,6-dicarboxylate lactonase (EC 3.1.1.57) is an enzyme that catalyzes the chemical reaction

2-pyrone-4,6-dicarboxylate + H₂O $\rightleftharpoons$ 4-carboxy-2-hydroxyhexa-2,4-dienedioate

Thus, the two substrates of this enzyme are 2-pyrone-4,6-dicarboxylate and H₂O, whereas its product is 4-carboxy-2-hydroxyhexa-2,4-dienedioate.

This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 2-pyrone-4,6-dicarboxylate lactonohydrolase. This enzyme participates in benzoate degradation via hydroxylation.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 3.1.1.57
BRENDA references for 3.1.1.57 (Recommended.)
PubMed references for 3.1.1.57
PubMed Central references for 3.1.1.57
Google Scholar references for 3.1.1.57
Kersten PJ, Dagley S, Whittaker JW, Arciero DM, Lipscomb JD (1982). "2-pyrone-4,6-dicarboxylic acid, a catabolite of gallic acids in Pseudomonas species". J. Bacteriol. 152: 1154–62. PMID 7142106.
Maruyama K (Tokyo). "Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase". J. Biochem.: 557–65. PMID 6841353.