Literature DB >> 7819278

Contribution of mutant analysis to the understanding of enzyme catalysis: the case of class A beta-lactamases.

A Matagne1, J M Frère.   

Abstract

Class A beta-lactamases represent a family of well studied enzymes. They are responsible for many antibiotic resistance phenomena and thus for numerous failures in clinical chemotherapy. Despite the facts that five structures are known at high resolution and that detailed analyses of enzymes modified by site-directed mutagenesis have been performed, their exact catalytic mechanism remains controversial. This review attempts to summarize and to discuss the many available data.

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Year:  1995        PMID: 7819278     DOI: 10.1016/0167-4838(94)00177-i

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  28 in total

1.  Active TEM-1 beta-lactamase mutants with random peptides inserted in three contiguous surface loops.

Authors:  Pascale Mathonet; Julie Deherve; Patrice Soumillion; Jacques Fastrez
Journal:  Protein Sci       Date:  2006-09-08       Impact factor: 6.725

2.  Recombination and selection can remove blaTEM alleles from bacterial populations.

Authors:  Joanna E Mroczkowska; Miriam Barlow
Journal:  Antimicrob Agents Chemother       Date:  2008-07-14       Impact factor: 5.191

Review 3.  Catalytic properties of class A beta-lactamases: efficiency and diversity.

Authors:  A Matagne; J Lamotte-Brasseur; J M Frère
Journal:  Biochem J       Date:  1998-03-01       Impact factor: 3.857

Review 4.  The other kind of biological NMR--studies of enzyme-substrate interactions.

Authors:  G C Roberts
Journal:  Neurochem Res       Date:  1996-09       Impact factor: 3.996

5.  Electrostatic steering and ionic tethering in enzyme-ligand binding: insights from simulations.

Authors:  R C Wade; R R Gabdoulline; S K Lüdemann; V Lounnas
Journal:  Proc Natl Acad Sci U S A       Date:  1998-05-26       Impact factor: 11.205

6.  Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine at position 69.

Authors:  P Giakkoupi; V Miriagou; M Gazouli; E Tzelepi; N J Legakis; L S Tzouvelekis
Journal:  Antimicrob Agents Chemother       Date:  1998-05       Impact factor: 5.191

7.  Construction and characterization of an OHIO-1 beta-lactamase bearing Met69Ile and Gly238Ser mutations.

Authors:  R A Bonomo; J R Knox; S D Rudin; D M Shlaes
Journal:  Antimicrob Agents Chemother       Date:  1997-09       Impact factor: 5.191

8.  A point mutation leads to altered product specificity in beta-lactamase catalysis.

Authors:  E R Lewis; K M Winterberg; A L Fink
Journal:  Proc Natl Acad Sci U S A       Date:  1997-01-21       Impact factor: 11.205

9.  Quantifying enzyme activity in living cells.

Authors:  Agnes Zotter; Felix Bäuerle; Debabrata Dey; Vladimir Kiss; Gideon Schreiber
Journal:  J Biol Chem       Date:  2017-08-07       Impact factor: 5.157

10.  Inhibition by Avibactam and Clavulanate of the β-Lactamases KPC-2 and CTX-M-15 Harboring the Substitution N132G in the Conserved SDN Motif.

Authors:  Clément Ourghanlian; Daria Soroka; Michel Arthur
Journal:  Antimicrob Agents Chemother       Date:  2017-02-23       Impact factor: 5.191

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