Understanding promiscuous amidase activity of an esterase from Bacillus subtilis

被引：53
|
作者：
Kourist, Robert [1 ]
Bartsch, Sebastian [1 ]
Fransson, Linda [2 ]
Hult, Karl [2 ]
Bornscheuer, Uwe T. [1 ]
机构：
[1] Ernst Moritz Arndt Univ Greifswald, Dept Biotechnol & Enzyme Catalysis, D-17487 Greifswald, Germany
[2] AlbaNova Univ Ctr, Dept Biochem, Sch Biotechnol, S-10691 Stockholm, Sweden
来源：
CHEMBIOCHEM | 2008年 / 9卷 / 01期
关键词：
amidases; Bacillus subtilis; catalysis; esterases; molecular modeling;
D O I：
10.1002/cbic.200700521
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：
Water works. Bacillus subtilis esterase BS2 is a promiscuous esterase that shows amidase activity. This amidase activity was shown to depend on a hydrogen-bond network with the substrate amide hydrogen (indicated by arrow). When this stabilising hydrogen bond network was removed by a point mutation, the amide activity was significantly lowered in comparison with the esterase activity. (Figure Presented) © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码：67 / 69
页数：3
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