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Glucose-6-phosphate isomerase.

A Achari, S E Marshall, H Muirhead

    Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
    |June 26, 1981
    PubMed
    Summary
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    Researchers determined the crystal structure of pig muscle glucose-6-phosphate isomerase, revealing its alpha/beta type structure and active site location. Sequence analysis identified a key lysine residue crucial for enzymatic activity.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Enzymology

    Background:

    • Glucose-6-phosphate isomerase (GPI) is a crucial dimeric enzyme (132,000 Da) catalyzing the interconversion of glucose-6-phosphate and fructose-6-phosphate.
    • Understanding GPI's structure is vital for elucidating its catalytic mechanism and potential therapeutic targets.

    Purpose of the Study:

    • To determine the crystal structure of pig muscle glucose-6-phosphate isomerase.
    • To identify key residues and structural features involved in enzyme activity.

    Main Methods:

    • X-ray crystallography was used to determine the enzyme's structure at 2.6 A resolution.
    • Cyanogen bromide cleavage was employed to generate peptide fragments for sequence analysis.
    • Peptide fragments were purified and sequenced, with tentative fitting to the electron density map.

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    Main Results:

    • The crystal structure revealed an alpha/beta type fold, with each subunit comprising two domains.
    • The active site is located at both the domain and subunit interfaces.
    • Sequence analysis of cyanogen bromide fragments identified a modified lysine residue critical for enzymatic activity.
    • A potential shared active site motif (histidine and glutamate) was proposed for GPI, triose phosphate isomerase, and pyruvate kinase.

    Conclusions:

    • The determined structure provides insights into the quaternary and tertiary structure of glucose-6-phosphate isomerase.
    • Identification of a critical lysine residue highlights its importance in catalysis.
    • The findings suggest potential structural similarities in the active sites of related isomerases and kinases.