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

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...

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Bibliografiske detaljer

Udgivet i:	J Bacteriol
Principais autores:	Hensgens, C M, Vonck, J, Van Beeumen, J, van Bruggen, E F, Hansen, T A
Format:	Artigo
Sprog:	Inglês
Udgivet:	American Society for Microbiology (ASM) 1993
Fag:	Research Article
Online adgang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC204602/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8491707/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.175.10.2859-2863.1993
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