Preliminary observations on alcohol dehydrogenases in Comamonas terrigena that exhibit stereospecificity towards secondary alcohols

Abstract

Extracts of the cells of Comamonas terrigena, grown under a variety of different conditions, contain two distinct, constitutive, NAD-dependent alcohol dehydrogenase enzymes that can be separated by polyacrylamide-gel electrophoresis. One of the enzymes exhibits activity towards D-alkan-2-ols and primary alcohols and the other is active towards L-alkan-2-ols, symmetrical secondary alcohols and probably other positional isomers of secondary alcohols of the L-configuration. Methods for the individual assay of the two enzymes have been developed and have been used to define some of their general properties. Most of the substrates for these enzymes would not support growth of C. terrigena under the experimental conditions used and were relatively poorly oxidized by resting cell suspensions.

Purification and Characterization of Two NAD-Dependent Alcohol Dehydrogenases (ADHs) Induced in the Quinoprotein ADH-Deficient Mutant ofAcetobacter pasteurianusSKU1108

“…ADHs reacting with secondary alcohol are obtained from methylotrophic bacteria or yeast. [22][23][24] Comamonas terrigena oxidize preferentially the R-(-)-stereoisomer, 25) whereas the Rhodococcus erythropolis enzyme is speciˆc for the S-(＋)-stereoisomer.…”

Purification and characterization of a chemotolerant alcohol dehydrogenase applicable to coupled redox reactions

“…Protein concentrations were measured according to the method of Bradford (1976). Native gel electrophoresis (Grell et al, 1965;Barrett et al, 1980;Ornstein, 1964;Davis, 1964) and SDS-page electrophoresis (Laemmli, 1970) were performed as described in the literature.…”

Degradation of 2-chloroethanol by wild type and mutants of Pseudomonas putida US2

“…The expression of these alcohol dehydrogenases enabled the strain to metabolise a wide range of different alcohols, indicating that the enzymes are probably not specifically involved in chloroethanol metabolism. Similar alcohol dehydrogenase systems have been described in the literature previously (Barrett et al 1980;Wyatt et al 1987). The PES-dependent alcohol dehydrogenase of strain US2 was inducible and ammonia was needed for optimal activity.…”