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

Emil Hamnevik; Dirk Maurer; Thilak Reddy Enugala; Thao Chu; Robin Löfgren; Doreen Dobritzsch; Mikael Widersten

doi:10.1021/acs.biochem.8b00055

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

Biochemistry. 2018 Feb 20;57(7):1059-1062. doi: 10.1021/acs.biochem.8b00055. Epub 2018 Feb 2.

Authors

Emil Hamnevik¹, Dirk Maurer¹, Thilak Reddy Enugala¹, Thao Chu¹, Robin Löfgren¹, Doreen Dobritzsch¹, Mikael Widersten¹

Affiliation

¹ Department of Chemistry-BMC, Uppsala University , Box 576, SE-751 23 Uppsala, Sweden.

PMID: 29384657
DOI: 10.1021/acs.biochem.8b00055

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alcohol Dehydrogenase / chemistry
Alcohol Dehydrogenase / genetics*
Alcohol Dehydrogenase / metabolism*
Catalytic Domain
Directed Molecular Evolution* / methods
Ethylene Glycols / chemistry
Ethylene Glycols / metabolism*
Fatty Alcohols / chemistry
Fatty Alcohols / metabolism*
Mutagenesis
Oxidation-Reduction
Protein Conformation
Rhodococcus / chemistry
Rhodococcus / enzymology*
Rhodococcus / genetics
Rhodococcus / metabolism
Stereoisomerism
Substrate Specificity

Substances

Ethylene Glycols
Fatty Alcohols
styrene glycol
acyloin
Alcohol Dehydrogenase