1,4-lactonase
| 1,4-lactonase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.1.25 | ||||||||
| CAS number | 37278-38-9 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a 1,4-lactonase (EC 3.1.1.25) is an enzyme that catalyzes the generic chemical reaction:
- a 1,4-lactone + H2O a 4-hydroxyacid
Thus, the two substrates of this enzyme are 1,4-lactone and H2O, whereas its product is 4-hydroxyacid.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 1,4-lactone hydroxyacylhydrolase. This enzyme is also called gamma-lactonase. This enzyme participates in galactose metabolism and ascorbate and aldarate metabolism. It employs one cofactor, calcium.
Structural studies
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes 2DG0, 2DG1, and 2DSO.
References
- Fishbein WN, Bessman SP (1966). "Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of gamma-lactones. I. Tissue localization, stoichiometry, specificity, distinction from esterase". J. Biol. Chem. 241 (21): 4835–41. PMID 4958984.
- Fishbein WN, Bessman SP (1966). "Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of gamma-lactones. II. Metal ion effects, kinetics, and equilibra". J. Biol. Chem. 241 (21): 4842–7. PMID 4958985.
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