Structural highlights
Publication Abstract from PubMed
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.
Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase.,Wang S, Nie Y, Xu Y, Zhang R, Ko TP, Huang CH, Chan HC, Guo RT, Xiao R Chem Commun (Camb). 2014 Jun 24;50(58):7770-2. doi: 10.1039/c4cc01752h. PMID:24834985[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang S, Nie Y, Xu Y, Zhang R, Ko TP, Huang CH, Chan HC, Guo RT, Xiao R. Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase. Chem Commun (Camb). 2014 Jun 24;50(58):7770-2. doi: 10.1039/c4cc01752h. PMID:24834985 doi:http://dx.doi.org/10.1039/c4cc01752h
