Directed Evolution of Alcohol Dehydrogenase for Improved Stereoselective Redox Transformations of 1-Phenylethane-1,2-diol and Its Corresponding Acyloin | Health & Environmental Research Online (HERO)

Health & Environmental Research Online (HERO)

Print Feedback Export to File

This record has one attached file:

Citation
Tags

HERO ID

4659305

Reference Type

Journal Article

Title

Directed Evolution of Alcohol Dehydrogenase for Improved Stereoselective Redox Transformations of 1-Phenylethane-1,2-diol and Its Corresponding Acyloin

Author(s)

Hamnevik, E; Maurer, D; Enugala, TR; Chu, T; Löfgren, R; Dobritzsch, D; Widersten, M

Year

2018

Is Peer Reviewed?

Yes

Journal

Biochemistry
ISSN: 0006-2960
EISSN: 1520-4995

Publisher

AMER CHEMICAL SOC

Location

WASHINGTON

Volume

Issue

Page Numbers

1059-1062

Language

English

PMID

29384657

DOI

10.1021/acs.biochem.8b00055

Web of Science Id

WOS:000426013300003

URL

https://www.scopus.com/inward/record.uri?eid=2-s2.0-85042280367&doi=10.1021%2facs.biochem.8b00055&partnerID=40&md5=c62185a3d1c9ac0d986d5824bdec9ca6
Exit

Abstract

Laboratory evolution of alcohol dehydrogenase produced enzyme variants with improved turnover numbers with a vicinal 1,2-diol and its corresponding hydroxyketone. Crystal structure and transient kinetics analysis aids in rationalizing the new functions of these variants.