1,4-lactonase
| 1,4-lactonase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.1.25 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
The enzyme 1,4-lactonase (EC 3.1.1.25) catalyzes the generic reaction
- a 1,4-lactone + H2O a 4-hydroxyacid
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 1,4-lactone hydroxyacylhydrolase. It is also called γ-lactonase. It participates in galactose metabolism and ascorbate and aldarate metabolism. It employs one cofactor, Ca2+.
Structural studies
[edit]As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes 2DG0, 2DG1, and 2DSO.
Applications
[edit]In a study by Chen et al. a 1,4-lactonase was expressed in E. coli and used as a highly efficient biocatalyst for asymmetric synthesis of chiral compounds.[1]
References
[edit]- ^ Chen, Bing; Fan, Li-Qiang; Xu, Jian-He; Zhao, Jian; Zhang, Xian; Ouyang, Li-Ming (October 2010). "Biocatalytic properties of a recombinant Fusarium proliferatum lactonase with significantly enhanced production by optimal expression in Escherichia coli". Applied Biochemistry and Biotechnology. 162 (3): 744–756. doi:10.1007/s12010-009-8819-1. ISSN 1559-0291. PMID 19876606.
- Fishbein WN, Bessman SP (1966). "Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of γ-lactones. I. Tissue localization, stoichiometry, specificity, distinction from esterase". J. Biol. Chem. 241 (21): 4835–41. doi:10.1016/S0021-9258(18)99641-9. 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 γ-lactones. II. Metal ion effects, kinetics, and equilibra". J. Biol. Chem. 241 (21): 4842–7. doi:10.1016/S0021-9258(18)99642-0. PMID 4958985.
