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D-apiose reductase from Aerobacter aerogenes.

D L Neal, P K Kindel

    Journal of Bacteriology
    |March 1, 1970
    PubMed
    Summary
    This summary is machine-generated.

    A new enzyme, d-apiose reductase, was discovered in Aerobacter aerogenes PRL-R3, which utilizes d-apiose as its sole carbon source. This enzyme catalyzes the interconversion of d-apiose and d-apiitol, dependent on nicotinamide adenine dinucleotide.

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    Area of Science:

    • Microbiology
    • Enzymology
    • Biochemistry

    Background:

    • Aerobacter aerogenes PRL-R3 utilizes d-apiose as its sole carbon source.
    • The metabolic pathways for d-apiose utilization were previously uncharacterized.

    Purpose of the Study:

    • To isolate and characterize a novel enzyme involved in d-apiose metabolism.
    • To elucidate the enzymatic mechanism and substrate specificity of the newly discovered enzyme.

    Main Methods:

    • Isolation of Aerobacter aerogenes PRL-R3 utilizing d-apiose.
    • Enzyme purification and characterization of d-apiose reductase.
    • Determination of kinetic parameters (K(m)) and cofactor specificity.
    • Enzymatic assays using paper chromatography for product identification.

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    Main Results:

    • Discovery of d-apiose reductase, an enzyme not present when grown on d-glucose.
    • The enzyme catalyzes the nicotinamide adenine dinucleotide-dependent interconversion of d-apiose and d-apiitol.
    • High specificity for d-apiose and d-apiitol, with K(m) values of 0.02 M and 0.01 M, respectively.
    • Optimal activity at pH 7.5 for d-apiose reduction and pH 10.5 for d-apiitol oxidation.
    • Enzyme remains soluble after high-speed centrifugation.

    Conclusions:

    • D-apiose reductase is a novel enzyme in Aerobacter aerogenes PRL-R3 crucial for d-apiose metabolism.
    • The enzyme exhibits specific substrate and cofactor requirements, indicating a distinct role in carbohydrate metabolism.
    • D-apiose and d-apiitol do not interact with other related dehydrogenases in the organism.