[HTML][HTML] Horse liver aldehyde dehydrogenase: II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity
RI Feldman, H Weiner - Journal of Biological Chemistry, 1972 - ASBMB
Aldehyde: NAD oxidoreductase (EC 1.2. 1.3), purified to homogeneity from horse liver,
possesses, in addition to its dehydrogenase activity, the ability to hydrolyze p-nitrophenyl
esters at a rate equal to approximately one-third that of the oxidation-reduction reaction. That
this esterase activity is most probably an active site phenomenon is suggested by the
competitive inhibition of nitrophenyl acetate hydrolysis by high concentrations of
propionaldehyde, a substrate for the dehydrogenase reaction. The coenzyme for the …
possesses, in addition to its dehydrogenase activity, the ability to hydrolyze p-nitrophenyl
esters at a rate equal to approximately one-third that of the oxidation-reduction reaction. That
this esterase activity is most probably an active site phenomenon is suggested by the
competitive inhibition of nitrophenyl acetate hydrolysis by high concentrations of
propionaldehyde, a substrate for the dehydrogenase reaction. The coenzyme for the …