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Article

Exploring the reversal of enantioselectivity on a zinc-dependent alcohol dehydrogenase.

Organic & biomolecular chemistry - 16 May 2017

Maria-Solano Miguel A, Romero-Rivera Adrian, Osuna Sílvia

Abstract excerpt

Alcohol Dehydrogenase (ADH) enzymes catalyse the reversible reduction of prochiral ketones to the corresponding alcohols. These enzymes present two differently shaped active site pockets, which dictate their substrate scope and selectivity. In this study, we computationally evaluate the effect of two commonly reported active site mutations (I86A, and W110T) on a secondary alcohol dehydrogenase from...

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Identifiers

PMID: 28436515
DOI: 10.1039/c7ob00482f
PMCID: PMC5436084

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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