Literature DB >> 23183431

R164H and V240H replacements by site-directed mutagenesis of TEM-149 extended-spectrum β-lactamase: kinetic analysis of TEM-149H240 and TEM-149H164-H240 laboratory mutants.

Mariagrazia Perilli1, Giuseppe Celenza, Paola Sandra Mercuri, Moreno Galleni, Cristina Pellegrini, Bernardetta Segatore, Gianfranco Amicosante.   

Abstract

Two laboratory mutant forms, TEM-149(H240) and TEM-149(H164-H240), of the TEM-149 extended-spectrum β-lactamase enzyme were constructed by site-directed mutagenesis. TEM-149(H240) and TEM-149(H164-H240) were similar in kinetic behavior, except with respect to benzylpenicillin and ceftazidime. Molecular modeling of the two mutant enzymes demonstrated the role of histidine at position 240 in the reduction of the affinity of the enzyme for ceftazidime.

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Year:  2012        PMID： 23183431      PMCID： PMC3553744          DOI： 10.1128/AAC.01268-12

Source DB:  PubMed          Journal:  Antimicrob Agents Chemother        ISSN： 0066-4804            Impact factor:   5.191


  8 in total

1.  Predicting evolutionary potential: in vitro evolution accurately reproduces natural evolution of the tem beta-lactamase.

Authors:  Miriam Barlow; Barry G Hall
Journal:  Genetics       Date:  2002-03       Impact factor: 4.562

Review 2.  Natural evolution of TEM-1 β-lactamase: experimental reconstruction and clinical relevance.

Authors:  Merijn L M Salverda; J Arjan G M De Visser; Miriam Barlow
Journal:  FEMS Microbiol Rev       Date:  2010-11       Impact factor: 16.408

3.  Biochemical analysis of TEM-134, a new TEM-type extended-spectrum beta-lactamase variant produced in a Citrobacter koseri clinical isolate from an Italian hospital.

Authors:  Mariagrazia Perilli; Giuseppe Celenza; Marianna Fiore; Bernardetta Segatore; Cristina Pellegrini; Francesco Luzzaro; Gian Maria Rossolini; Gianfranco Amicosante
Journal:  J Antimicrob Chemother       Date:  2007-08-02       Impact factor: 5.790

4.  E240V substitution increases catalytic efficiency toward ceftazidime in a new natural TEM-type extended-spectrum beta-lactamase, TEM-149, from Enterobacter aerogenes and Serratia marcescens clinical isolates.

Authors:  Mariagrazia Perilli; Giuseppe Celenza; Francesca De Santis; Cristina Pellegrini; Chiara Forcella; Gian Maria Rossolini; Stefania Stefani; Gianfranco Amicosante
Journal:  Antimicrob Agents Chemother       Date:  2007-12-26       Impact factor: 5.191

Review 5.  beta-Lactamases: protein evolution in real time.

Authors:  J Petrosino; C Cantu; T Palzkill
Journal:  Trends Microbiol       Date:  1998-08       Impact factor: 17.079

6.  Site-directed mutagenesis by overlap extension using the polymerase chain reaction.

Authors:  S N Ho; H D Hunt; R M Horton; J K Pullen; L R Pease
Journal:  Gene       Date:  1989-04-15       Impact factor: 3.688

Review 7.  Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure.

Authors:  J R Knox
Journal:  Antimicrob Agents Chemother       Date:  1995-12       Impact factor: 5.191

Review 8.  Extended-spectrum beta-lactamases: a clinical update.

Authors:  David L Paterson; Robert A Bonomo
Journal:  Clin Microbiol Rev       Date:  2005-10       Impact factor: 26.132
  8 in total
  1 in total

1.  Kinetic study of the effect of histidines 240 and 164 on TEM-149 enzyme probed by β-lactam inhibitors.

Authors:  Mariagrazia Perilli; Alisia Mancini; Giuseppe Celenza; Carlo Bottoni; Pierangelo Bellio; Alessia Sabatini; Letizia Di Pietro; Fabrizia Brisdelli; Bernardetta Segatore; Gianfranco Amicosante
Journal:  Antimicrob Agents Chemother       Date:  2014-08-04       Impact factor: 5.191
  1 in total

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