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Updated: Apr 25, 2026

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity
Published on: March 25, 2020
Engineering of highly selective variants of Parvibaculum lavamentivorans alcohol dehydrogenase
Dominik Spickermann1, Sascha Hausmann, Christian Degering
1evocatal GmbH, Alfred-Nobel-Strasse 10, 40789 Monheim am Rhein (Germany).
Abstract:
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 % (wild-type) to ≥99 % and concomitantly to enhance conversion by 43.5 %.

