Literature DB >> 590269

The peptidoglycan crosslinking enzyme system in Streptomyces strains R61, K15 and rimosus. Kinetic coefficients involved in the interactions of the membrane-bound transpeptidase with peptide substrates and beta-lactam antibiotics.

J Dusart, M Leyh-Bouille, J M Ghuysen.   

Abstract

The transpeptidation reaction performed by the membranes of Streptomyces strain R61 fits the general rate equation for an enzyme-catalysed bimolecular reaction. The same membranes (E) interact with beta-lactams (I) to form inactive penicillin-enzyme-membrane complexes (EI) of rather high stability, which subsequently break down (E + I leads to EI leads to E + degradation products). The enzyme is regenerated and the antibiotic is released in the form of an inactive metabolite. With benzylpenicillin, the degradation product is benzylpenicilloic acid. The reaction is heat-labile. The first step of the reaction (E + I leads to EI) is characterized by a second-order rate constant (kformation in M-1 s-1) and the second step (EI leads to E + degradation products) by a first-order rate constant (kbreakdown in s-1). The effects in vitro of various beta-lactams on the membrane-bound transpeptidase, as expressed by the relevant kformation and kbreakdown values, parallel the effects in vivo of the same antibiotics as expressed by their ability to prevent the germination and growth of conidiospores. The kinetic parameters of the transpeptidase that was solubilized with N-cetyl-N,N,N-trimethylammonium bromide with respect to its interaction with both peptide substrates and beta-lactam antibiotics are quantitatively different from those of the membrane-bound enzyme. Moreover, the solubilized enzyme fragments benzylpenicillin with formation of phenylacetylglycine, a reaction which is similar to that catalysed by the exocellular R61 enzyme. The membranes of Streptomyces strains rimosus and K15 possess an active 'classic' penicillinase. They were not studied but the kinetic coefficients of the corresponding solubilized transpeptidases were determined and compared with those of the solubilized enzyme from strain R61.

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Year:  1977        PMID: 590269     DOI: 10.1111/j.1432-1033.1977.tb11924.x

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


  6 in total

1.  Visualization of penicillin-binding proteins during sporulation of Streptomyces griseus.

Authors:  J Hao; K E Kendrick
Journal:  J Bacteriol       Date:  1998-04       Impact factor: 3.490

Review 2.  Epidemiology of β-Lactamase-Producing Pathogens.

Authors:  Karen Bush; Patricia A Bradford
Journal:  Clin Microbiol Rev       Date:  2020-02-26       Impact factor: 26.132

3.  Effects of nucleophiles on the breakdown of the benzylpenicilloyl-enzyme complex EI formed between benzylpenicillin and the exocellular DD-carboxypeptidase--transpeptiase of Streptomyces strain R61.

Authors:  A Marquet; J M Frère; J M Ghuysen; A Loffet
Journal:  Biochem J       Date:  1979-03-01       Impact factor: 3.857

4.  Isolation of the membrane-bound 26 000-Mr penicillin-binding protein of Streptomyces strain K15 in the form of a penicillin-sensitive D-alanyl-D-alanine-cleaving transpeptidase.

Authors:  M Nguyen-Distèche; M Leyh-Bouille; J M Ghuysen
Journal:  Biochem J       Date:  1982-10-01       Impact factor: 3.857

5.  Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.

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

Review 6.  Activities and regulation of peptidoglycan synthases.

Authors:  Alexander J F Egan; Jacob Biboy; Inge van't Veer; Eefjan Breukink; Waldemar Vollmer
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2015-10-05       Impact factor: 6.237

  6 in total

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