PMID: 7030736Oct 1, 1981Paper

Stereospecificity and other properties of a novel secondary-alcohol-specific alcohol dehydrogenase

European Journal of Biochemistry
C T HouI Marczak

Abstract

NAD-dependent alcohol dehydrogenase from the methanol-grown Methylcoccus sp. CRL M1 (type I membrane), Methylosinus trichosporium OB3b (type II membrane), Methylobacterium organophillum CRL 26 (type II membrane, facultative methylotroph). Pseudomonas sp. ATCC 21439, and Pichia pastoris Y-55 are secondary-alcohol-specific and that from P. pastoris Y-7556 is not. This novel secondary-alcohol-specific alcohol dehydrogenase (secondary-alcohol dehydrogenase) has been purified from methanol-grown Pseudomonas sp. ATCC 21439. Secondary-alcohol dehydrogenase shows a single protein band on acrylamide gel electrophoresis and has a molecular weight of 95000. It consists of two subunits of Mr 48000 daltons and two atoms of zinc per molecule of enzyme protein. It oxidizes secondary alcohols, notably 2-propanol and 2-butanol. Primary alcohols are not oxidized. The pH and temperature optima for secondary-alcohol dehydrogenase are 8--9, and 30--35 degrees C, respectively. The activation energy calculated is 82.8 kJ. Secondary-alcohol dehydrogenase also catalyzes the reduction of methyl ketones to their corresponding 2-alcohols in the presence of NADH (a reverse reaction). The Km values at 25 degrees C in the forward reaction for 2-butanol, (2R)...Continue Reading

References

Apr 1, 1978·Journal of Bacteriology·W G NiehausE A Kingsley
Jul 13, 1972·Biochimica Et Biophysica Acta·J P Tassin, J P Vandecasteele
May 1, 1963·Journal of Bacteriology·H B LUKINS, J W FOSTER

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Citations

May 15, 2003·Archives of Biochemistry and Biophysics·Ronald Bentley
Nov 20, 2016·Scientific Reports·Vijayalakshmi KandasamyPeter Ruhdal Jensen
May 23, 2014·Applied Microbiology and Biotechnology·Enriqueta Martinez-RojasLeif-Alexander Garbe

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