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Lactate dehydrogenase in Phycomyces blakesleeanus

J Soler, D De Arriaga, F Busto

    The Biochemical Journal
    |May 1, 1982
    PubMed
    Summary
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    This study purified lactate dehydrogenase from Phycomyces blakesleeanus, revealing complex substrate and coenzyme interactions. The enzyme

    Area of Science:

    • Biochemistry
    • Enzymology
    • Mycology

    Background:

    • Lactate dehydrogenase (LDH) is a key enzyme in cellular metabolism.
    • Understanding LDH kinetics and regulation is crucial for metabolic studies.

    Purpose of the Study:

    • To purify and characterize NAD-specific L(+)-lactate dehydrogenase from Phycomyces blakesleeanus.
    • To investigate the enzyme's kinetic properties, including substrate and coenzyme interactions and regulatory mechanisms.

    Main Methods:

    • Purification of lactate dehydrogenase from Phycomyces blakesleeanus mycelium.
    • Enzyme activity assays at varying pH, substrate, and coenzyme concentrations.
    • Polyacrylamide-gel electrophoresis for purity assessment.
    • Kinetic analysis of enzyme inhibition and activation.

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    Main Results:

    • A ~700-fold purified NAD-specific L(+)-lactate dehydrogenase was obtained with a molecular weight of 135,000-140,000.
    • The enzyme exhibited optimal activity between pH 6.7 and 7.5.
    • Homotropic interactions with pyruvate and NADH were observed at pH 7.5, suggesting multiple binding sites.
    • Substrate inhibition by pyruvate occurred at pH 6.0, with 3-hydroxypyruvate and 2-oxovalerate showing analogous effects.
    • ATP acted as a competitive inhibitor with NADH and pyruvate at pH 7.5, but allosterically inhibited NADH at pH 6.0.
    • GTP had no effect on enzyme activity under tested conditions.

    Conclusions:

    • Phycomyces blakesleeanus lactate dehydrogenase displays complex regulatory behavior.
    • The enzyme's kinetics are pH-dependent, influencing its interaction with substrates, coenzymes, and inhibitors.
    • These findings contribute to understanding fungal metabolic pathways and enzyme regulation.