1,4-lactonase
| 1,4-lactonase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.1.25 | ||||||||
| CAS no. | 37278-38-9 | ||||||||
| 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 | ||||||||
| |||||||||
1,4-lactonase (EC 3.1.1.25) is an enzyme that catalyzes the generic reaction
- a 1,4-lactone + H2O a 4-hydroxyacid
For example, the enzyme characterised from human blood and rat liver microsomes gives the sugar acid, D-galactonic acid by hydrolyis of D-galactono-1,4-lactone:[1][2][3]
D-galactono-1,4-lactone
H2O
D-galactonic acid
This enzyme is a hydrolase, specifically one acting on carboxylic ester bonds. The systematic name is 1,4-lactone hydroxyacylhydrolase. It is also called γ-lactonase. It requires calcium as Ca2+.[4]
Structural studies
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes PDB: 2DG0, PDB: 2DG1, and PDB: 2DSO.
Applications
A 1,4-lactonase was expressed in Escherichia coli and used as a highly efficient biocatalyst for asymmetric synthesis of chiral compounds.[5]
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 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.
- ↑ Schomburg, Dietmar; Salzmann, Margit (1991). "1, 4-Lactonase". Enzyme Handbook 3. pp. 107–109. doi:10.1007/978-3-642-76463-9_21. ISBN 978-3-642-48962-4.
- ↑ Enzyme 3.1.1.25 at KEGG Pathway Database.
- ↑ 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.