Literature DB >> 6346347

N,O-diacylhydroxylamines as enzyme-activated inhibitors for serine proteases.

G Fischer, H U Demuth, A Barth.   

Abstract

Several N-peptidyl-O(4-nitrobenzoyl)-hydroxylamines were synthesized and their inhibitory action against dipeptidyl-peptidase IV, alpha-chymotrypsin, elastase and thermitase was investigated. If the petidyl residue can be recognized by the enzyme as a substrate, a time dependent irreversible inactivation occurs. The mechanism of inhibition by N,O-diacylhydroxylamines as enzyme activated inhibitors is discussed.

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Year:  1983        PMID： 6346347     DOI： 10.1002/chin.198341334

Source DB:  PubMed          Journal:  Pharmazie        ISSN： 0031-7144            Impact factor:   1.267


  3 in total

1.  Potent and selective inactivation of cysteine proteinases with N-peptidyl-O-acyl hydroxylamines.

Authors:  D Brömme; A Schierhorn; H Kirschke; B Wiederanders; A Barth; S Fittkau; H U Demuth
Journal:  Biochem J       Date:  1989-11-01       Impact factor: 3.857

2.  Inhibition of dipeptidyl peptidase IV by fluoroolefin-containing N-peptidyl-O-hydroxylamine peptidomimetics.

Authors:  J Lin; P J Toscano; J T Welch
Journal:  Proc Natl Acad Sci U S A       Date:  1998-11-24       Impact factor: 11.205

3.  Dipeptidyl peptidase IV of human lymphocytes. Evidence for specific hydrolysis of glycylproline p-nitroanilide in T-lymphocytes.

Authors:  E Schön; H U Demuth; A Barth; S Ansorge
Journal:  Biochem J       Date:  1984-10-01       Impact factor: 3.857
  3 in total

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