Abstract
A NAD-dependent, oxygen-labile alcohol dehydrogenase was purified from Desulfovibrio gigas. It was decameric, with subunits of M(r) 43,000. The best substrates were ethanol (K(m), 0.15 mM) and 1-propanol (K(m), 0.28 mM). N- terminal amino acid sequence analysis showed that the enzyme belongs to the same family of alcohol dehydrogenases as Zymomonas mobilis ADH2 and Bacillus methanolicus MDH.
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CITATION STYLE
Hensgens, C. M. H., Vonck, J., Van Beeumen, J., Van Bruggen, E. F. J., & Hansen, T. A. (1993). Purification and characterization of an oxygen-labile, NAD-dependent alcohol dehydrogenase from Desulfovibrio gigas. Journal of Bacteriology, 175(10), 2859–2863. https://doi.org/10.1128/jb.175.10.2859-2863.1993
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