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Article

Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity.

Journal of molecular biology - 17 Jun 2005

Schlieben Nils Helge, Niefind Karsten, Müller Jörg, Riebel Bettina, Hummel Werner, Schomburg Dietmar

Abstract excerpt

The R-specific alcohol dehydrogenase (RADH) from Lactobacillus brevis is an NADP-dependent, homotetrameric member of the extended enzyme family of short-chain dehydrogenases/reductases (SDR) with a high biotechnological application potential. Its preferred in vitro substrates are prochiral ketones like acetophenone with almost invariably a small methyl group as one substituent and a bulky (often aromatic) moiety...

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Identifiers

PMID: 15896805
DOI: 10.1016/j.jmb.2005.04.029

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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