Bovine lens aldehyde dehydrogenase. Kinetics and mechanism.
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.
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D000444:Aldehyde Dehydrogenase; D000445:Aldehyde Oxidoreductases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002697:Chloral Hydrate / Q000378:metabolism; D007700:Kinetics; D007908:Lens, Crystalline / Q000201:enzymology*; D009243:NAD / Q000031:analogs & derivatives / Q000378:metabolism; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000494:pharmacology; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D013438:Sulfhydryl Compounds; D013439:Sulfhydryl Reagents; D009243:NAD; D000246:Adenosine Diphosphate Ribose; C003451:thionicotinamide adenine dinucleotide; D002697:Chloral Hydrate; D000445:Aldehyde Oxidoreductases; D000444:Aldehyde Dehydrogenase