The oxidation of aldehydes by horse liver alcohol dehydrogenase.
A lag phase in the spectrophotometric assay progress curve of aldehyde oxidation by HL-ADH was observed and characterised. The aldehyde oxidation and aldehyde dismutation reactions were shown to be related, and a mechanism to explain net aldehyde oxidation was proposed. The spectrophotometric assay was shown to be unsuitable for measurement of kinetic parameters for aldehyde oxidation by HL-ADH, and kinetic constants previously determined were shown to be in error. Existing data on the aldehyde dismutation reaction are insufficient to discount a role for HL-ADH in aldehyde transformation in vivo.
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446.
G T
GT
Henehan
G L
GL
Kenyon
N J
NJ
Oppenheimer
D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism*; D000818:Animals; D006736:Horses; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity
D000447:Aldehydes; D009243:NAD; D000426:Alcohol Dehydrogenase; C018475:butyraldehyde; C031639:caprylic aldehyde