Literature DB >> 7106103

Interaction between monobactams and Streptomyces R61 DD-carboxypeptidase.

N H Georgopapadakou, S A Smith, C M Cimarusti.   

Abstract

The monobactams are a novel family of monocyclic beta-lactam antibiotics characterized by the 2-oxoazetidine-1-sulfonic acid moiety. A series of monobactams bind covalently to the Streptomyces R61 DD-carboxypeptidase in a manner similar to that for bicyclic beta-lactams, especially cephalosporins. The similarity of interaction was established by the following criteria: inhibition of binding by diisopropylfluorophosphate and alpha-dicarbonyls; stoichiometry of binding; similarity of partial proteolysis products of radiolabelled enzyme; rates of release of bound beta-lactams; nature of hydrolysis and hydroxylaminolysis products.

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Year:  1982        PMID: 7106103     DOI: 10.1111/j.1432-1033.1982.tb06622.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  Interaction of (2,3)-methylenepenams with penicillin-binding proteins.

Authors:  N H Georgopapadakou; D A Russo; A Liebman; W Burger; P Rossman; D Keith
Journal:  Antimicrob Agents Chemother       Date:  1987-07       Impact factor: 5.191

2.  Streptomyces K15 DD-peptidase-catalysed reactions with suicide beta-lactam carbonyl donors.

Authors:  M Leyh-Bouille; M Nguyen-Distèche; S Pirlot; A Veithen; C Bourguignon; J M Ghuysen
Journal:  Biochem J       Date:  1986-04-01       Impact factor: 3.857

3.  Binding of monobactams to penicillin-binding proteins of Escherichia coli and Staphylococcus aureus: relation to antibacterial activity.

Authors:  N H Georgopapadakou; S A Smith; C M Cimarusti; R B Sykes
Journal:  Antimicrob Agents Chemother       Date:  1983-01       Impact factor: 5.191

  3 in total

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