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The microsomal dicarboxylyl-CoA synthetase.

J Vamecq, E de Hoffmann, F Van Hoof

    The Biochemical Journal
    |September 15, 1985
    PubMed
    Summary

    Rat liver dicarboxylyl-CoA synthetase activates dicarboxylic acids (C5-C16) to CoA esters. This enzyme, found in microsomes, is inhibited by AMP and PPi, and its activity parallels in vivo degradation.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Metabolic Pathways

    Background:

    • Dicarboxylic acids are metabolic products of monocarboxylic acid omega-oxidation.
    • Understanding the metabolism of dicarboxylic acids is crucial for comprehending lipid metabolism.

    Purpose of the Study:

    • To investigate the activation and subsequent catabolism of dicarboxylic acids in rat liver.
    • To identify and characterize the enzyme responsible for dicarboxylic acid activation.

    Main Methods:

    • Enzyme assays using dicarboxylic acids (C5-C16) as substrates.
    • ATP-dependent CoA ester formation measurement.
    • Feedback inhibition studies with AMP and PPi.
    • Cell fractionation to determine enzyme localization.
    • Monitoring H2O2 production to assess oxidase activity.

    Main Results:

    • A dicarboxylyl-CoA synthetase was identified in rat liver microsomes, activating dicarboxylic acids (C5-C16) to their CoA esters.
    • The enzyme utilizes ATP, converting it to AMP and PPi, which act as feedback inhibitors.
    • Dicarboxylyl-CoA synthetase is thermolabile at 37°C, optimal at pH 6.5, with highest activity on dodecanedioic acid.
    • An oxidase system was discovered that processes dicarboxylyl-CoA esters, indicated by H2O2 production.
    • The chain-length specificity of this pathway mirrors in vivo dicarboxylic acid degradation.

    Conclusions:

    • Rat liver possesses a specific pathway for dicarboxylic acid catabolism involving activation to CoA esters and subsequent oxidation.
    • Dicarboxylyl-CoA synthetase is a key enzyme in this pathway, localized to hepatic microsomes.
    • The identified pathway's substrate specificity suggests its significant role in the overall handling of dicarboxylic acids.

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