Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase
Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase
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不保守的底物结合位点指导中链醇脱氢酶的立体选择性
DOI：
10.1039/c4cc01752h
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发表时间：
2014
影响因子：
4.9
通讯作者：
Rong Xiao
中科院分区：
文献类型：
--
作者：
Shanshan Wang;Yao Nie;Yan Xu;Rongzhen Zhang;Tzu-Ping Ko;Chun-Hsiang Huang;Hsiu-Chien Chan;Rey-Ting Guo;Rong Xiao
底物结合口袋的结构导向设计逆转了NADH依赖性中链醇脱氢酶（MDR）从Prelog到anti-Prelog的立体选择性。口袋形成氨基酸，特别是作为热点的非保守残基，在指导MDR的立体选择性中起关键作用。
Structure-guided design of substrate-binding pocket inversed the stereoselectivity of an NADH-dependent medium-chain alcohol dehydrogenase (MDR) from Prelog to anti-Prelog. The pocket-forming amino acids, especially the unconserved residues as hotspots, play critical roles in directing MDRs' stereoselectivity.