Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase.
The dissociation of the aldehyde dehydrogenase X NADH complex was studied by displacement with NAD+. The association reaction of enzyme and NADH was also studied. These processes are biphasic, as shown by McGibbon, Buckley & Blackwell [(1977) Biochem. J. 165, 455-462], but the details of the dissociation reaction are significantly different from those given by those authors. Spectral and kinetic experiments provide evidence for the formation of abortive complexes of the type enzyme X NADH X aldehyde. Kinetic studies at different wavelengths with transcinnamaldehyde as substrate provide evidence for the formation of an enzyme X NADH X cinnamoyl complex. Hydrolysis of the thioester relieves a severe quenching effect on the fluorescence of enzyme-bound NADH.
D000171:Acrolein / Q000031:analogs & derivatives / Q000378:metabolism; D000444:Aldehyde Dehydrogenase / Q000378:metabolism*; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D009243:NAD / Q000378:metabolism; D012756:Sheep; D013050:Spectrometry, Fluorescence
D046911:Macromolecular Substances; D009243:NAD; D000171:Acrolein; D000444:Aldehyde Dehydrogenase; C012843:cinnamaldehyde