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Related Experiment Videos

An active site peptide from pepsin C.

J Kay, A P Ryle

    The Biochemical Journal
    |June 1, 1971
    PubMed
    Summary

    Porcine pepsin C is irreversibly inactivated by a specific inhibitor, diazoacetyl-dl-norleucine methyl ester, at pH 4.5. This reaction targets an active site aspartic acid residue, crucial for enzyme function.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Chemistry

    Background:

    • Porcine pepsin C is a digestive enzyme.
    • Understanding enzyme inactivation mechanisms is vital for biochemical research and pharmaceutical development.
    • Specific inhibitors are used to probe enzyme active sites.

    Purpose of the Study:

    • To investigate the inactivation mechanism of porcine pepsin C using diazoacetyl-dl-norleucine methyl ester.
    • To identify the specific residue and location within the enzyme that reacts with the inhibitor.
    • To compare the active site sequence with that of pepsin.

    Main Methods:

    • Enzyme inactivation assays with diazoacetyl-dl-norleucine methyl ester and cupric ions.
    • Quantification of inhibitor incorporation into the enzyme.
    • Amino acid sequencing to identify the reaction site.

    Main Results:

    • Porcine pepsin C is rapidly and irreversibly inactivated above pH 4.5.
    • Inactivation involves the incorporation of one mole of inhibitor residue per mole of enzyme.
    • The reaction site is the beta-carboxyl group of an aspartic acid residue in the Ile-Val-Asp-Thr sequence.
    • This sequence is identical to the active site sequence in pepsin.

    Conclusions:

    • The study identifies a specific aspartic acid residue in the active site of porcine pepsin C as the target for inactivation.
    • The findings highlight the structural similarity between porcine pepsin C and pepsin active sites.
    • This research contributes to understanding the structure-function relationship of aspartic proteases.

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