Affiliation:
1. Department of Microbiology, University of Groningen, Haren, The Netherlands.
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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
46 articles.
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