当前位置： SCI文献检索 > JOURNAL OF BIOTECHNOLOGY期刊下所有文献 > Towards the computational design and engineering of enzyme enantioselectivity: A case study by a carbonyl reductase from Gluconobacter oxydans.

Towards the computational design and engineering of enzyme enantioselectivity: A case study by a carbonyl reductase from Gluconobacter oxydans.

Abstract：

:In our previous work, a NAD(H)-dependent carbonyl reductase (GoCR) was identified from Gluconobacter oxydans, which showed moderate to high enantiospecificity for the reduction of different kinds of prochiral ketones. In the present study, the crystal structure of GoCR was determined at 1.65Å resolution, and a computational strategy concerning substrate-enzyme docking and all-atom molecular dynamics (MD) simulation was established to help understand the molecular basis of enantiopreference and enantiorecognition for GoCR, and to further guide the design and engineering of GoCR enantioselectivity. For the reduction of ethyl 2-oxo-4-phenylbutyrate (OPBE), three binding pocket residues, Cys93, Tyr149, and Trp193 were predicted to play a critical role in determining the enantioselectivity. Through site-directed mutagenesis, single-point mutant W193A was constructed and proved to reduce OPBE to ethyl (R)-2-hydroxy-4-phenylbutyrate (R-HPBE) with a significantly improved ee of >99% compared to 43.2% for the wild type (WT). Furthermore, double mutant C93V/Y149A was proved to even invert the enantioselectivity of GoCR to afford S-HPBE at 79.8% ee.

journal_name

J Biotechnol

journal_title

Journal of biotechnology

authors

Deng J,Yao Z,Chen K,Yuan YA,Lin J,Wei D

doi

10.1016/j.jbiotec.2015.11.003

subject

Has Abstract

pub_date

2016-01-10 00:00:00

pages

31-40

eissn

0168-1656

issn

1873-4863

pii

S0168-1656(15)30175-9

journal_volume

217

pub_type

杂志文章

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