Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase.
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.
School of Biotechnology and Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China. yxu@jiangnan.edu.cn.
Shanshan
S
Wang
Yao
Y
Nie
Yan
Y
Xu
Rongzhen
R
Zhang
Tzu-Ping
TP
Ko
Chun-Hsiang
CH
Huang
Hsiu-Chien
HC
Chan
Rey-Ting
RT
Guo
Rong
R
Xiao
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D001665:Binding Sites; D006801:Humans; D062105:Molecular Docking Simulation; D013237:Stereoisomerism
D000426:Alcohol Dehydrogenase