Article
Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer.
The FEBS journal - 1 Nov 2017
Hamnevik Emil, Enugala Thilak Reddy, Maurer Dirk, Ntuku Siphosethu, Oliveira Ana, Dobritzsch Doreen, Widersten Mikael
Abstract excerpt
Alcohol dehydrogenase A (ADH-A) from Rhodococcus ruber DSM 44541 is a promising biocatalyst for redox transformations of arylsubstituted sec-alcohols and ketones. The enzyme is stereoselective in the oxidation of 1-phenylethanol with a 300-fold preference for the (S)-enantiomer. The low catalytic efficiency with (R)-1-phenylethanol has been attributed to nonproductive binding of this substrate at the active site....
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