Expanding the Substrate Specificity of Thermoanaerobacter pseudoethanolicus Secondary Alcohol Dehydrogenase by a Dual Site Mutation

Musa M. Musa, Odey Bsharat, Ibrahim Karume, Claire Vieille, Masateru Takahashi, Samir Hamdan

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

Here, we report the asymmetric reduction of selected phenyl-ring-containing ketones by various single and dual site mutants of Thermoanaerobacter pseudoethanolicus secondary alcohol dehydrogenase (TeSADH). Further expanding the size of the substrate binding pocket in the mutant W110A/I86A not only allowed substrates of the single mutants W110A and I86A to be accommodated within the expanded active site, but also expanded the enzyme's substrate range to ketones bearing two sterically demanding groups (bulky-bulky ketones), which are not substrates for TeSADH single mutants. We also report the regio- and enantioselective reduction of diketones using W110A/I86A TeSADH and single TeSADH mutants. The double mutant exhibited dual stereopreference generating the Prelog products most of the time and the anti-Prelog products in a few cases.
Original languageEnglish (US)
Pages (from-to)798-805
Number of pages8
JournalEuropean Journal of Organic Chemistry
Volume2018
Issue number6
DOIs
StatePublished - Feb 13 2018

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