Isolation of a highly enantioselective epoxide hydrolase from Rhodococcus sp. NCIMB 11216 |
| |
| Authors: | Martin Mischitz Kurt Faber Andrew Willetts |
| |
| Affiliation: | (1) Institute of Organic Chemistry, Graz University of Technology, Stremayrgasse 16, A-8010 Graz, Austria;(2) Department of Biological Sciences, Exeter University, EX4 4QG Exeter, UK |
| |
| Abstract: | Summary Whole cells of Rhodococcus sp. NCIMB 11216 catalyze the asymmetric hydrolysis of racemic epoxides giving access to chiral epoxides and diols, which are important chiral building blocks for the synthesis of bioactive compounds. Employing a four-step purification procedure, the epoxide hydrolase responsible for the reaction was isolated and characterized to be a cofactor-independent, soluble monomeric protein of ~35kDa, exhibiting an isoelectric point of 4.7. |
| |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ |
|
