Literature DB >> 8964456

An additional ionic bond suggested by molecular modelling of TEM-2 might induce a slight discrepancy between catalytic properties of TEM-1 and TEM-2 beta-lactamases.

E B Chaïbi1, S Farzaneh, J Péduzzi, M Barthélémy, R Labia.   

Abstract

The plasmid-mediated TEM-1 and TEM-2 beta-lactamases are the most commonly encountered among Gram-negative bacteria. They belong to molecular class A, and differ by one amino acid at position 39:TEM-1 have a glutamine and TEM-2 a lysine. Kinetic parameters (kcat and Km) and catalytic efficiency (kcat/Km) of TEM-1 and TEM-2 beta-lactamases are slightly, but significantly different. For all antibiotics except methicillin and cefazolin, the catalytic efficiency values of TEM-2 are clearly greater than that of TEM-1. Molecular modelling of TEM-2, when compared to that of TEM-1, showed an additional ionic bond between Lys-39 and Glu-281.

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Year:  1996        PMID： 8964456     DOI： 10.1016/0378-1097(96)00304-7

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN： 0378-1097            Impact factor:   2.742


  5 in total

Review 1.  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

2.  Selection of naturally occurring extended-spectrum TEM beta-lactamase variants by fluctuating beta-lactam pressure.

Authors:  J Blazquez; M I Morosini; M C Negri; F Baquero
Journal:  Antimicrob Agents Chemother       Date:  2000-08       Impact factor: 5.191

3.  A novel extended-spectrum TEM-type beta-lactamase (TEM-52) associated with decreased susceptibility to moxalactam in Klebsiella pneumoniae.

Authors:  C Poyart; P Mugnier; G Quesne; P Berche; P Trieu-Cuot
Journal:  Antimicrob Agents Chemother       Date:  1998-01       Impact factor: 5.191

4.  Properties of IRT-14 (TEM-45), a newly characterized mutant of TEM-type beta-lactamases.

Authors:  M M Caniça; M Barthélémy; L Gilly; R Labia; R Krishnamoorthy; G Paul
Journal:  Antimicrob Agents Chemother       Date:  1997-02       Impact factor: 5.191

5.  Network models of TEM β-lactamase mutations coevolving under antibiotic selection show modular structure and anticipate evolutionary trajectories.

Authors:  Violeta Beleva Guthrie; Jennifer Allen; Manel Camps; Rachel Karchin
Journal:  PLoS Comput Biol       Date:  2011-09-22       Impact factor: 4.475
  5 in total

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