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Proline specific endo- and exopeptidases

R Walter, W H Simmons, T Yoshimoto

    Molecular and Cellular Biochemistry
    |April 18, 1980
    PubMed
    Summary
    This summary is machine-generated.

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    This study reviews proline-specific peptidases, including endopeptidases and exopeptidases. It discusses their properties, characteristics, and significance in biological processes.

    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Proline residues are unique in peptide bonds due to their cyclic structure.
    • Specific enzymes, termed peptidases, are responsible for cleaving peptide bonds involving proline.

    Purpose of the Study:

    • To comprehensively review proline-specific peptidases.
    • To discuss their properties, distinguishing characteristics, and biological significance.

    Main Methods:

    • Literature review of proline-specific peptidases.
    • Classification of peptidases based on cleavage site (endo-, N-terminal exo-, C-terminal exo-, dipeptidases).

    Main Results:

    • Detailed description of various proline-specific peptidases, including post-proline cleaving enzyme, proline specific endopeptidase, post-proline dipeptidyl aminopeptidase, proline iminopeptidase, aminopeptidase P, prolylcarboxypeptidase, carboxypeptidase P, prolyl dipeptidase, and proline dipeptidase.

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  • Discussion of enzymes that hydrolyze proline-containing bonds but are not proline-specific.

    • Conclusions:

    • Proline-specific peptidases play diverse roles in biological systems.
    • Understanding these enzymes is crucial for various biochemical and physiological processes.