Obtaining Optical Purity for Product Diols in Enzyme-Catalyzed Epoxide Hydrolysis: Contributions from Changes in both Enantio- and Regioselectivity

Autor:	Huan Ma, Paul Bauer, Åsa Janfalk Carlsson, Mikael Widersten
Rok vydání:	2012
Předmět:	Stereochemistry Hydrolysis Epoxide Regioselectivity Stereoisomerism Directed evolution Biochemistry Catalysis Enzymes Kinetics chemistry.chemical_compound chemistry Epoxy Compounds Organic chemistry Enantiomer Chirality (chemistry) Enantiomeric excess Epoxide hydrolase Saturated mutagenesis
Zdroj:	Biochemistry. 51:7627-7637
ISSN:	1520-4995 0006-2960
DOI:	10.1021/bi3007725
Popis:	Enzyme variants of the plant epoxide hydrolase StEH1 displaying improved stereoselectivities in the catalyzed hydrolysis of (2,3-epoxypropyl)benzene were generated by directed evolution. The evolution was driven by iterative saturation mutagenesis in combination with enzyme activity screenings where product chirality was the decisive selection criterion. Analysis of the underlying causes of the increased diol product ratios revealed two major contributing factors: increased enantioselectivity for the corresponding epoxide enantiomer(s) and, in some cases, a concomitant change in regioselectivity in the catalyzed epoxide ring-opening half-reaction. Thus, variant enzymes that catalyzed the hydrolysis of racemic (2,3-epoxypropyl)benzene into the R-diol product in an enantioconvergent manner were isolated.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::143756e412f44d07776364ebf49b83d3 https://doi.org/10.1021/bi3007725 Zobrazit plný text záznamu