Literature DB >> 2205241

A new look at Pz-peptidase.

A J Barrett1.   

Abstract

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.

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Year:  1990        PMID: 2205241

Source DB:  PubMed          Journal:  Biol Chem Hoppe Seyler        ISSN: 0177-3593


  2 in total

1.  A quenched fluorescent substrate for thimet peptidase containing a new fluorescent amino acid, DL-2-amino-3-(7-methoxy-4-coumaryl)propionic acid.

Authors:  C G Knight
Journal:  Biochem J       Date:  1991-02-15       Impact factor: 3.857

2.  Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase.

Authors:  A J Barrett; M A Brown
Journal:  Biochem J       Date:  1990-11-01       Impact factor: 3.857

  2 in total

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