期刊
CHEMISTRYSELECT
卷 1, 期 4, 页码 836-839出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/slct.201600254
关键词
epoxidation; peroxides; enzyme; industrial catalysis; protein structure
资金
- National Science Funds for the Excellent Youth Scholars [31222043]
- Science and Technology planning project of Guangdong province [2014B020204003]
Lipases show high stability in lipophilic solvents and catalyze reactions at the water-oil interfaces, which are of great industrial interest. One promising application of lipases is the production of epoxides from alkenes and hydrogen peroxide. So far, little attention has been given to uncover the reaction mechanism for this in detail at the molecular level. Here, we present structural and mutational analysis of a lipase from Penicillium camembertii that indicates a two-stage synergistic mechanism for this reaction. Surprisingly, a mutant devoid of the catalytic serine retains a fraction of activity while histidine from the catalytic triad is absolutely critical to maintain the enzyme activity. Histidine appears to perform a dual-activation role acting both towards hydrogen peroxide and the catalytic serine. These results thus allow a better understanding of enzymatic epoxidation and engineering of more potent, stable and selective enzymes.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据