Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase.

Biochemical characterization of recombinant benzyl alcohol dehydrogenase from Rhodococcus ruber UKMP-5M

Benzyl Alcohol Dehydrogenase (BADH) is an important enzyme for hydrocarbon degradation, which can oxidize benzyl alcohols to aldehydes, while being capable of catalyzing a reversible reaction by reducing benzaldehyde. BADH is a member of medium chain alcohol dehydrogenases, in which zinc and NAD are essential for enzyme activity. This paper describes the expression, purification, and characteri...

Biochemical characterization of recombinant benzyl alcohol dehydrogenase from Rhodococcus ruber UKMP-5M

Benzyl Alcohol Dehydrogenase (BADH) is an important enzyme for hydrocarbon degradation, which can oxidize benzyl alcohols to aldehydes, while being capable of catalyzing a reversible reaction by reducing benzaldehyde. BADH is a member of medium chain alcohol dehydrogenases, in which zinc and NAD are essential for enzyme activity. This paper describes the expression, purification, and characteri...

Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer.

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 ...

The influence of pH on the substrate specificity and stereoselectivity of alcohol dehydrogenase from horse liver.

Promiscuous Substrate-Binding Explains the Enzymatic Stereo- and Regiocontrolled Synthesis of Enantiopure Hydroxy Ketones and Diols

Regioand stereoselective reductions of several diketones to afford enantiopure hydroxy ketones or diols were accomplished using isolated alcohol dehydrogenases (ADHs). Results could be rationalised taking into account different (promiscuous) substrate-binding modes in the active site of the enzyme. Furthermore, interesting natural cyclic diketones were also reduced with high regioand stereosele...