Microbiological transformations 50: selection of epoxide hydrolases for enzymatic resolution of 2-, 3- or 4-pyridyloxirane

被引：23

作者：

Genzel, Y

Archelas, A

Broxterman, QB

Schulze, B

Furstoss, R

机构：

[1] Univ Mediterranee, Grp Biocatalyse & Chim Fine, UMR 6111, CNRS,Fac Sci Luminy, F-13288 Marseille 9, France

[2] DSM Fine Chem Adv Synth & Catalysis, NL-6160 MD Geleen, Netherlands

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2002年 / 16卷 / 5-6期

关键词：

epoxide hydrolases; enzymatic resolution; Aspergillus niger; pyridyloxirane; screening;

D O I：

10.1016/S1381-1177(01)00064-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A study aimed to select efficient epoxide hydrolases (EHs) allowing to achieve the enzymatic resolution of 2-, 3- and 4-pyridyloxirane (1-3) has been achieved, using 2-pyridyloxirane I as test substrate. Five thus selected EH-sources that showed interesting enantioselectivity were looked at in more detail for the conversion of 1-3. (C) 2002 Elsevier Science B.V. All rights reserved.

引用

页码：217 / 222

页数：6

共 38 条

[1] Cloning and molecular characterization of a soluble epoxide hydrolase from Aspergillus niger that is related to mammalian microsomal epoxide hydrolase [J].