Back to Search
Start Over
Cloning, expression, and characterization of an anti-Prelog stereospecific carbonyl reductase from Gluconobacter oxydans DSM2343.
- Source :
-
Enzyme & Microbial Technology . Mar2015, Vol. 70, p18-27. 10p. - Publication Year :
- 2015
-
Abstract
- A new anti-Prelog stereospecific carbonyl reductase (GoKR) from Gluconobacter oxydans DSM2343 was cloned and identified in Escherichia coli . This GoKR formed a homo-tetramer with a subunit size of approximately 27.0 kDa. GoKR exhibited full activity with NADPH but not with NADH as a cofactor. The optimal pH and temperature were 9.0 and 30 °C, respectively. GoKR reduced various ketones, including aliphatic and aromatic ketones, α- and β-keto esters. Aromatic ketones were reduced to ( R )-enantiomers, whereas keto esters were reduced to ( S )-hydroxy esters with different enantioselectivities. The data indicate that GoKR does not obey Prelog's rule and exhibits anti-Prelog enantiopreference. Enzyme–substrate–cofactor docking analysis showed that hydride transfer occurred at the si faces of carbonyl group for ethyl 4-chloro-3-oxobutanoate (COBE), which was then selectively reduced to the chiral ( S )-alcohol. Excellent enantioselectivities were obtained for reducing COBE and ethyl 2-oxo-4-phenylbutyrate into the corresponding ( S )-type products. These products are important for synthesizing HMG-CoA reductase (statins) and angiotensin-converting enzyme inhibitors, respectively. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 01410229
- Volume :
- 70
- Database :
- Academic Search Index
- Journal :
- Enzyme & Microbial Technology
- Publication Type :
- Academic Journal
- Accession number :
- 100874589
- Full Text :
- https://doi.org/10.1016/j.enzmictec.2014.12.004