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. 1985 Jan 1;225(1):159–165. doi: 10.1042/bj2250159

Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase.

F M Dickinson
PMCID: PMC1144564  PMID: 3977822

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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