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Literature DB >> 23006757

The sequence-activity relationship between metallo-β-lactamases IMP-1, IMP-6, and IMP-25 suggests an evolutionary adaptation to meropenem exposure.

Eleanor M Liu¹, Kevin M Pegg, Peter Oelschlaeger.

Abstract

Metallo-β-lactamases are important determinants of antibacterial resistance. In this study, we investigate the sequence-activity relationship between the closely related enzymes IMP-1, IMP-6, and IMP-25. While IMP-1 is the more efficient enzyme across the overall spectrum of tested β-lactam antibacterial agents, IMP-6 and IMP-25 seem to have evolved to specifically inactivate the newer carbapenem meropenem. Molecular modeling indicates that the G235S mutation distinguishing IMP-25 from IMP-1 and IMP-6 may affect enzyme activity via Asn233.

Entities: Chemical Gene Mutation

Mesh：

Substances：

Year: 2012 PMID： 23006757 PMCID： PMC3497198 DOI： 10.1128/AAC.01440-12

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

28 in total

1. Plasmid-encoded metallo-beta-lactamase (IMP-6) conferring resistance to carbapenems, especially meropenem.

Authors: H Yano; A Kuga; R Okamoto; H Kitasato; T Kobayashi; M Inoue
Journal: Antimicrob Agents Chemother Date: 2001-05 Impact factor: 5.191

2. In vitro evolution predicts that the IMP-1 metallo-beta-lactamase does not have the potential to evolve increased activity against imipenem.

Authors: Barry G Hall
Journal: Antimicrob Agents Chemother Date: 2004-03 Impact factor: 5.191

3. Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase.

Authors: J H Toney; G G Hammond; P M Fitzgerald; N Sharma; J M Balkovec; G P Rouen; S H Olson; M L Hammond; M L Greenlee; Y D Gao
Journal: J Biol Chem Date: 2001-06-04 Impact factor: 5.157

4. Amino acid substitutions in a variant of IMP-1 metallo-beta-lactamase.

Authors: S Iyobe; H Kusadokoro; J Ozaki; N Matsumura; S Minami; S Haruta; T Sawai; K O'Hara
Journal: Antimicrob Agents Chemother Date: 2000-08 Impact factor: 5.191

Review 5. Appropriate empirical antibacterial therapy for nosocomial infections: getting it right the first time.

Authors: Marin Kollef
Journal: Drugs Date: 2003 Impact factor: 9.546

6. Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor.

Authors: N O Concha; C A Janson; P Rowling; S Pearson; C A Cheever; B P Clarke; C Lewis; M Galleni; J M Frère; D J Payne; J H Bateson; S S Abdel-Meguid
Journal: Biochemistry Date: 2000-04-18 Impact factor: 3.162

7. Comparative stability studies of antipseudomonal beta-lactams for potential administration through portable elastomeric pumps (home therapy for cystic fibrosis patients) and motor-operated syringes (intensive care units).

Authors: Eric Viaene; Hugues Chanteux; Hélène Servais; Marie-Paule Mingeot-Leclercq; Paul M Tulkens
Journal: Antimicrob Agents Chemother Date: 2002-08 Impact factor: 5.191

8. Modeling domino effects in enzymes: molecular basis of the substrate specificity of the bacterial metallo-beta-lactamases IMP-1 and IMP-6.

Authors: Peter Oelschlaeger; Rolf D Schmid; Juergen Pleiss
Journal: Biochemistry Date: 2003-08-05 Impact factor: 3.162

9. Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance.

Authors: E Osano; Y Arakawa; R Wacharotayankun; M Ohta; T Horii; H Ito; F Yoshimura; N Kato
Journal: Antimicrob Agents Chemother Date: 1994-01 Impact factor: 5.191

10. Insight into the mechanism of the IMP-1 metallo-beta-lactamase by molecular dynamics simulations.

Authors: Peter Oelschlaeger; Rolf D Schmid; Jürgen Pleiss
Journal: Protein Eng Date: 2003-05

14 in total

1. Biochemical characterization of IMP-30, a metallo-β-lactamase with enhanced activity toward ceftazidime.

Authors: Kevin M Pegg; Eleanor M Liu; Alecander E Lacuran; Peter Oelschlaeger
Journal: Antimicrob Agents Chemother Date: 2013-07-08 Impact factor: 5.191

Review 2. B1-Metallo-β-Lactamases: Where Do We Stand?

Authors: Maria F Mojica; Robert A Bonomo; Walter Fast
Journal: Curr Drug Targets Date: 2016 Impact factor: 3.465

3. Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: the importance of residue 262.

Authors: Kevin M Pegg; Eleanor M Liu; Alex C George; Alecander E LaCuran; Christopher R Bethel; Robert A Bonomo; Peter Oelschlaeger
Journal: Protein Sci Date: 2014-08-20 Impact factor: 6.725

4. Carbapenem Use Is Driving the Evolution of Imipenemase 1 Variants.

Authors: Zishuo Cheng; Christopher R Bethel; Pei W Thomas; Ben A Shurina; John-Paul Alao; Caitlyn A Thomas; Kundi Yang; Steven H Marshall; Huan Zhang; Aidan M Sturgill; Andrea N Kravats; Richard C Page; Walter Fast; Robert A Bonomo; Michael W Crowder
Journal: Antimicrob Agents Chemother Date: 2021-03-18 Impact factor: 5.191

5. Susceptibility of Imipenem-Susceptible but Meropenem-Resistant bla_IMP-6-Carrying Enterobacteriaceae to Various Antibacterials, Including the Siderophore Cephalosporin Cefiderocol.

Authors: Sachi Kanazawa; Takafumi Sato; Naoki Kohira; Tsukasa Ito-Horiyama; Masakatsu Tsuji; Yoshinori Yamano
Journal: Antimicrob Agents Chemother Date: 2017-06-27 Impact factor: 5.191