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Structure-function relationships in lactate dehydrogenase.

M J Adams, M Buehner, K Chandrasekhar

    Proceedings of the National Academy of Sciences of the United States of America
    |July 1, 1973
    PubMed
    Summary
    This summary is machine-generated.

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    Lactate dehydrogenase (EC 1.1.1.27) enzyme structure reveals how coenzyme and substrate binding occurs. Specific protein interactions position the substrate for L-lactate specificity.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Enzymology

    Background:

    • Lactate dehydrogenase (LDH) is a crucial enzyme in cellular metabolism.
    • Understanding LDH's structure-function relationship is key to elucidating its catalytic mechanisms.

    Purpose of the Study:

    • To analyze the binding of coenzyme and substrate to lactate dehydrogenase.
    • To correlate binding interactions with the enzyme's known primary and tertiary structure.

    Main Methods:

    • Analysis of protein structure and coenzyme/substrate binding interactions.
    • Consideration of amino acid residues involved in active site binding.

    Main Results:

    • The coenzyme's adenine binds in a hydrophobic crevice, with phosphates interacting with the protein.

    Related Experiment Videos

  • Arginine 101 and other charged groups facilitate loop collapse, positioning the nicotinamide within a hydrophobic environment.
  • Substrate binding is influenced by histidine 195, arginine 171, and the nicotinamide ring, suggesting L-lactate specificity.

    • Conclusions:

    • The detailed spatial arrangement of the active site dictates substrate specificity for L-lactate.
    • Protein-coenzyme and protein-substrate interactions are critical for lactate dehydrogenase function.