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.
Research Article| November 01 1983
Bovine lens aldehyde dehydrogenase. Kinetics and mechanism
Biochem J (1983) 215 (2): 361–368.
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H H Ting, M J C Crabbe; Bovine lens aldehyde dehydrogenase. Kinetics and mechanism. Biochem J 1 November 1983; 215 (2): 361–368. doi: https://doi.org/10.1042/bj2150361
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