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. 1983 Nov 1;215(2):361–368. doi: 10.1042/bj2150361

Bovine lens aldehyde dehydrogenase. Kinetics and mechanism.

H H Ting, M J Crabbe
PMCID: PMC1152404  PMID: 6651766

Abstract

Bovine lens cytoplasmic aldehyde dehydrogenase exhibits Michaelis-Menten kinetics with acetaldehyde, glyceraldehyde 3-phosphate, p-nitrobenzaldehyde, propionaldehyde, glycolaldehyde, glyceraldehyde, phenylacetylaldehyde and succinic semialdehyde as substrates. The enzyme was also active with malondialdehyde, and exhibited an esterase activity. Steady-state kinetic analyses show that the enzyme exhibits a compulsory-ordered ternary-complex mechanism with NAD+ binding before acetaldehyde. The enzyme was inhibited by disulfiram and by p-chloromercuribenzoate, and studies with with mercaptans indicated the involvement of thiol groups in catalysis.

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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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