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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| Pubblicato in: | J Bacteriol |
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| Autori principali: | , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Microbiology (ASM)
1993
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| Soggetti: | |
| Accesso online: | 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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