1887

Abstract

Summary: strain JOB-5 cultured in the presence of propane contained an inducible secondary alcohol dehydrogenase. The enzyme was purified 198-fold using DEAE-cellulose, -aminopentyl agarose and NAD-agarose chromatography. The of the enzyme was approximately 136000, with subunits of 37000. The pH optimum for the reaction oxidizing propan-2-ol to propanone was 10–10.5 while the optimum for the reverse reaction was 7.5–8.5. The isoelectric point was 4.9. NAD but not NADP could serve as electron acceptor. The apparent values for propan-2-ol and NAD were 4.9 × 10M and 2.8 × 10 M, respectively. The enzyme was inhibited by thiol reagents and metal chelators. It appears to play an essential role in the metabolism of propane by this bacterium.

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1985-11-01
2022-01-21
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