A new look at Pz-peptidase.
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.
Department of Biochemistry, Strangeways Research Laboratory, Cambridge, England.
A J
AJ
Barrett
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D010450:Endopeptidases / Q000032:analysis* / Q000378:metabolism; D006801:Humans; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000494:pharmacology; D013045:Species Specificity; D013379:Substrate Specificity
D011480:Protease Inhibitors; D010450:Endopeptidases; D008666:Metalloendopeptidases; C022510:thimet oligopeptidase