Literature DB >> 25092695

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

Mariagrazia Perilli1, Alisia Mancini2, Giuseppe Celenza2, Carlo Bottoni2, Pierangelo Bellio2, Alessia Sabatini2, Letizia Di Pietro2, Fabrizia Brisdelli2, Bernardetta Segatore2, Gianfranco Amicosante2.   

Abstract

In the present study, we performed a detailed kinetic analysis of the enzymes TEM-149, TEM-149(H240), and TEM-149(H164-H240) versus a large panel of inhibitors/inactivators, including penicillins, penems, carbapenems, monobactams, cephamycin, and carbacephem. These compounds behaved as poor substrates versus TEM-149, TEM-149(H240), and TEM-149(H164-H240) β-lactamases, and the Ki (inhibition constant), K (dissociation constant of the Henri-Michaelis complex), k+2 and k+3 (first-order acylation and deacylation constants, respectively), and k+2/K values were calculated.
Copyright © 2014, American Society for Microbiology. All Rights Reserved.

Entities:  

Mesh：

Substances：

Year:  2014        PMID： 25092695      PMCID： PMC4187899          DOI： 10.1128/AAC.02950-14

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


  12 in total

Review 1.  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

2.  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

3.  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 4.  beta-Lactamases: protein evolution in real time.

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

5.  Automated analysis of enzyme inactivation phenomena. Application to beta-lactamases and DD-peptidases.

Authors:  F De Meester; B Joris; G Reckinger; C Bellefroid-Bourguignon; J M Frère; S G Waley
Journal:  Biochem Pharmacol       Date:  1987-07-15       Impact factor: 5.858

6.  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.

Authors:  Mariagrazia Perilli; Giuseppe Celenza; Paola Sandra Mercuri; Moreno Galleni; Cristina Pellegrini; Bernardetta Segatore; Gianfranco Amicosante
Journal:  Antimicrob Agents Chemother       Date:  2012-11-26       Impact factor: 5.191

7.  In vitro activity of CP-65,207, a new penem antimicrobial agent, in comparison with those of other agents.

Authors:  T Gootz; J Retsema; A Girard; E Hamanaka; M Anderson; S Sokolowski
Journal:  Antimicrob Agents Chemother       Date:  1989-08       Impact factor: 5.191

8.  In vitro activity of HRE 664, a penem antibiotic.

Authors:  X N Chin; H C Neu
Journal:  Diagn Microbiol Infect Dis       Date:  1990 Nov-Dec       Impact factor: 2.803

9.  Use of the chromosomal class A beta-lactamase of Mycobacterium fortuitum D316 to study potentially poor substrates and inhibitory beta-lactam compounds.

Authors:  M Galleni; N Franceschini; B Quinting; L Fattorini; G Orefici; A Oratore; J M Frère; G Amicosante
Journal:  Antimicrob Agents Chemother       Date:  1994-07       Impact factor: 5.191

10.  Kinetic and physical studies of beta-lactamase inhibition by a novel penem, BRL 42715.

Authors:  T H Farmer; J W Page; D J Payne; D J Knowles
Journal:  Biochem J       Date:  1994-11-01       Impact factor: 3.857
View more
  1 in total

1.  A Two Amino Acid Duplication, L167E168, in the Ω-Loop Drastically Decreases Carbapenemase Activity of KPC-53, a Natural Class A β-Lactamase.

Authors:  Alessandra Piccirilli; Sabrina Cherubini; Giuseppe Celenza; Gian Maria Rossolini; Fabrizia Brisdelli; Bernardetta Segatore; Luigi Principe; Francesco Luzzaro; Lilia Andriani; Gianfranco Amicosante; Mariagrazia Perilli
Journal:  Antimicrob Agents Chemother       Date:  2022-06-01       Impact factor: 5.938
  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.