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. 1993 May;175(10):2859–2863. doi: 10.1128/jb.175.10.2859-2863.1993

Purification and characterization of an oxygen-labile, NAD-dependent alcohol dehydrogenase from Desulfovibrio gigas.

C M Hensgens 1, J Vonck 1, J Van Beeumen 1, E F van Bruggen 1, T A Hansen 1
PMCID: PMC204602  PMID: 8491707

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 (Km, 0.15 mM) and 1-propanol (Km, 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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Selected References

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