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 family of alcohol dehydrogenases as Zymomonas mobilis ADH2 and Bacillus methanolicus MDH.
Hensgens
C M
CM
Department of Microbiology, University of Groningen, Haren, The Netherlands.
Vonck
J
J
Van Beeumen
J
J
van Bruggen
E F
EF
Hansen
T A
TA
D000426:Alcohol Dehydrogenase / Q000187:drug effects / Q000302:isolation & purification / Q000502:physiology* / Q000648:ultrastructure; D000595:Amino Acid Sequence; D003901:Desulfovibrio / Q000201:enzymology*; D008969:Molecular Sequence Data; D010100:Oxygen / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid
D000426:Alcohol Dehydrogenase; D010100:Oxygen