1,4-lactonase
1,4-lactonase | |||||||||
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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 | ||||||||
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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 .
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 . 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.
Applications[]
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[]
- ^ 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 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.
- EC 3.1.1
- Calcium enzymes
- Enzymes of known structure
- EC 3.1 stubs