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.
Department of Microbiology, University of Groningen, Haren, The Netherlands.
C M
CM
Hensgens
J
J
Vonck
J
J
Van Beeumen
E F
EF
van Bruggen
T A
TA
Hansen
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