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Human liver aldehyde dehydrogenase. Esterase activity.

R S Sidhu, A H Blair

    The Journal of Biological Chemistry
    |October 10, 1975
    PubMed
    Summary
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    Human liver aldehyde dehydrogenase exhibits esterase activity, hydrolyzing p-nitrophenyl esters. This dual function occurs at the same active site, influenced by pyridine nucleotides like NAD+ and NADH.

    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Human liver aldehyde dehydrogenase (ALDH) is primarily known for its role in alcohol metabolism.
    • Aldehyde dehydrogenases catalyze the oxidation of aldehydes to carboxylic acids.

    Purpose of the Study:

    • To investigate the esterase activity of human liver aldehyde dehydrogenase.
    • To determine if esterase and dehydrogenase activities are catalyzed by the same enzyme.
    • To elucidate the mechanism of ester hydrolysis by ALDH.

    Main Methods:

    • Enzyme kinetics studies using p-nitrophenyl acetate as a substrate.
    • Ion exchange chromatography and affinity chromatography to assess enzyme properties.
    • Competitive inhibition assays with known ALDH inhibitors.
    • Kinetic analysis of esterase activity in the presence of pyridine nucleotides (NAD+, NADH).

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    Main Results:

    • Human liver aldehyde dehydrogenase demonstrated significant p-nitrophenyl ester hydrolysis activity.
    • Esterase and dehydrogenase activities showed identical ion exchange and affinity properties, confirming a single protein.
    • Competitive inhibition studies indicated ester hydrolysis occurs at the aldehyde binding site.
    • NAD+ and NADH modulated esterase activity, with NAD+ causing a >5-fold acceleration and NADH a 2-fold increase.

    Conclusions:

    • Human liver aldehyde dehydrogenase possesses dual esterase and dehydrogenase functions.
    • Both activities are catalyzed by the same enzyme at the aldehyde binding site.
    • Pyridine nucleotides play a crucial role in modulating the esterase activity of ALDH.