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Phosphorylase: control and activity.

J A Jenkins, L N Johnson, D I Stuart

    Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
    |June 26, 1981
    PubMed
    Summary
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    Crystallographic studies reveal structural similarities between glycogen phosphorylase b and lactate dehydrogenase. Investigations into inhibitor binding sites provide insights into the catalytic mechanism involving pyridoxal phosphate.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Enzymology

    Background:

    • Glycogen phosphorylase b is a key enzyme in glycogen metabolism.
    • Understanding its structure and function is crucial for metabolic research.

    Purpose of the Study:

    • To review recent crystallographic findings on glycogen phosphorylase b.
    • To elucidate structural similarities with other enzymes and describe cofactor binding sites.

    Main Methods:

    • X-ray crystallography at 2 Å and 3 Å resolution.
    • Comparative structural analysis.

    Main Results:

    • Identified structural similarity in a 150-residue fold between phosphorylase and lactate dehydrogenase.
    • Described NADH binding sites in phosphorylase.

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  • Studied the crystal binding of glucose-1,2-cyclic phosphate, comparing it with glucose-1-phosphate binding.

    • Conclusions:

    • Structural insights support proposals for a catalytic mechanism involving pyridoxal phosphate.
    • Comparative analysis deepens understanding of enzyme structure-function relationships.