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Cytoplasmic malic enzyme from mouse kidneys.

C Y Lee, J H Yuan, D Moser

    Molecular and Cellular Biochemistry
    |November 30, 1978
    PubMed
    Summary
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    Researchers purified mouse kidney cytoplasmic malic enzyme (CME). Biochemical characterization revealed its tetrameric structure, kinetic properties, and stability, showing similarities to other species.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Molecular Biology

    Background:

    • Cytoplasmic malic enzyme (CME) plays a crucial role in cellular metabolism.
    • Understanding the biochemical properties of CME from different species can provide insights into metabolic regulation.
    • Previous studies have characterized CME from various sources, but detailed analysis from mouse kidney is limited.

    Purpose of the Study:

    • To purify NADP+-dependent cytoplasmic malic enzyme from mouse kidneys.
    • To characterize the biochemical properties of the purified mouse kidney CME.
    • To compare the properties of mouse kidney CME with those of CME from other species.

    Main Methods:

    • Enzyme purification using affinity chromatography (8-(6-aminohexyl)-amino-2', 5'-ADP-Sepharose) and ion exchange chromatography (DEAE-Sephadex).

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  • Biochemical characterization including molecular weight determination, amino acid composition analysis, steady-state kinetics, and thermal stability assays.
  • Enzyme inactivation studies using iodoacetate and urea.

    • Main Results:

    • The NADP+-dependent cytoplasmic malic enzyme was successfully purified to homogeneity from DBA/2J mouse kidneys.
    • The native enzyme is a tetramer with a molecular weight of approximately 270,000 Da.
    • Kinetic parameters (Km values for NADP+, L-malate, NADPH, and pyruvate) were determined, indicating an ordered kinetic mechanism with initial coenzyme binding, similar to pigeon liver CME. The enzyme showed weak inhibition by ATP and other metabolites. Amino acid composition showed high similarity to rat liver malic enzyme.

    Conclusions:

    • The purification and characterization of mouse kidney CME provide valuable biochemical data.
    • The enzyme's properties, including its ordered kinetic mechanism and structural similarity to other mammalian CME, highlight its conserved function in metabolism.
    • This study contributes to a deeper understanding of malic enzyme function and regulation in mammals.