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A new look at Pz-peptidase
1Department of Biochemistry, Strangeways Research Laboratory, Cambridge, England.
Biological Chemistry Hoppe-Seyler
|May 1, 1990
Summary
Pz-peptidase is a metallo-endopeptidase closely related to endo-oligopeptidase A. New research suggests its primary role is intracellular, not in connective tissue degradation.
Area of Science:
- Biochemistry
- Enzymology
Background:
- Pz-peptidase is a metallo-endopeptidase.
- Its function in connective tissue degradation is debated.
Purpose of the Study:
- To investigate the relationship between Pz-peptidase, soluble metallo-endopeptidase, and endo-oligopeptidase A.
- To elucidate the primary function of Pz-peptidase.
Main Methods:
- Utilized new quenched fluorescence substrates for Pz-peptidase.
- Employed inhibitors designed for soluble metallo-endopeptidase.
Main Results:
- Pz-peptidase, soluble metallo-endopeptidase, and endo-oligopeptidase A are likely identical or closely related.
- Pz-peptidase exhibits thiol-dependence.
- Orlowski's inhibitors are effective for Pz-peptidase studies.
- Limited evidence supports a role in connective tissue degradation.
Conclusions:
- Pz-peptidase is a thiol-dependent metallo-endopeptidase.
- Its main function is likely intracellular.