Understanding promiscuous amidase activity of an esterase from Bacillus subtilis
Understanding promiscuous amidase activity of an esterase from Bacillus subtilis
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DOI：
10.1002/cbic.200700521
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发表时间：
2008-01-04
期刊：
影响因子：
3.2
通讯作者：
Bornscheuer, Uwe T.
中科院分区：
文献类型：
--
作者：
Kourist, Robert;Bartsch, Sebastian;Bornscheuer, Uwe T.
水很管用枯草芽孢杆菌酯酶BS 2是一种具有酰胺酶活性的混杂酯酶。该酰胺酶活性显示依赖于与底物酰胺氢的氢键网络（由箭头指示）。当通过点突变去除这种稳定氢键网络时，与酯酶活性相比，酰胺活性显著降低。（图为）
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)