Barrett A J
Department of Biochemistry, Strangeways Research Laboratory, Cambridge, England.
Biol Chem Hoppe Seyler. 1990 May;371 Suppl:311-20.
Work with new, quenched fluorescence substrates of Pz-peptidase has led to the discovery that Pz-peptidase, soluble metallo-endopeptidase and endo-oligopeptidase A are either identical, or very closely related enzymes. Pz-peptidase is a metallo-endopeptidase with marked thiol-dependence. It has been confirmed that inhibitors of the type designed by Orlowski for soluble metallo-endopeptidase are effective tools in studying Pz-peptidase. There is little evidence to support the proposed role of Pz-peptidase in connective tissue matrix degradation, and the main function of the enzyme may be intracellular.
