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Article

Engineering of highly selective variants of Parvibaculum lavamentivorans alcohol dehydrogenase.

Chembiochem : a European journal of chemical biology - 22 Sept 2014

Spickermann Dominik, Hausmann Sascha, Degering Christian, Schwaneberg Ulrich, Leggewie Christian

Abstract excerpt

We present the development of highly selective variants of the Parvibaculum lavamentivorans alcohol dehydrogenase. Four amino acids (A158, N162, K202, L224) in the second sphere of the catalytic site were identified to determine the selectivity for 3-quinuclidone reduction significantly. The best variant (A158H/N162G/K202Q/L224W) was able to increase the ee for (R)-3-quinuclidinol production from 84.3 %...

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Identifiers

PMID: 25169816
DOI: 10.1002/cbic.201402216

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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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