Harnessing enzyme promiscuity of alditol-2-dehydrogenases for oxidation of alditols to enantiopure ketoses.

ABSTRACT: Several alditol-2-dehydrogenase enzymes from the short chain dehydrogenase (SDR) family catalyze the production of enantiopure rare ketoses from alditols as substrates and are used in biotech industry. Clearly, the absolute configuration of the internal chiral carbons in the open-chain conformation of alditols provides the structural basis for the enzymatic operation. This also allows for substrate ambiguity that manifest as enzyme promiscuity due to partial stereoselectivity of the enzyme. The issue is to make the right choice of a promiscuous enzyme and access maximum product diversity. Based on the absolute configuration of a cohort of ten enantiopure hexitols, this study is a systematic exploration of the stereochemical foundation of enzyme promiscuity in alditol-2-dehydrogenases which

SUBMITTER: De P 

PROVIDER: S-EPMC12193009 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature