Document Detail


Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-beta-lactamase IMP-1 produced by Escherichia coli.
MedLine Citation:
PMID:  10103197     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The blaIMP gene coding for the IMP-1 metallo-beta-lactamase produced by a Pseudomonas aeruginosa clinical isolate (isolate 101/1477) was overexpressed via a T7 expression system in Escherichia coli BL21 (DE3), and its product was purified to homogeneity with a final yield of 35 mg/liter of culture. The structural and functional properties of the enzyme purified from E. coli were identical to those of the enzyme produced by P. aeruginosa. The IMP-1 metallo-beta-lactamase exhibits a broad-spectrum activity profile that includes activity against penicillins, cephalosporins, cephamycins, oxacephamycins, and carbapenems. Only monobactams escape its action. The enzyme activity was inhibited by metal chelators, of which 1,10-o-phenanthroline and dipicolinic acid were the most efficient. Two zinc-binding sites were found. The zinc content of the P. aeruginosa 101/1477 metallo-beta-lactamase was not pH dependent.
Authors:
N Laraki; N Franceschini; G M Rossolini; P Santucci; C Meunier; E de Pauw; G Amicosante; J M Frère; M Galleni
Related Documents :
21824817 - Activity and stability enhancement of α-amylase treated with sub- and supercritical car...
16819907 - Purification and characterization of two novel beta-galactosidases from lactobacillus r...
411517 - Hydroxysteroid dehydrogenases of pseudomonas testosteroni. separation of a 17 beta-hydr...
3836017 - Lysosomal enzymes in human platelets.
24316447 - Cloning, overexpression and characterization of a thermostable pullulanase from thermus...
368587 - Analysis of regulatory mechanisms controlling the activity of the hexitol transport sys...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Antimicrobial agents and chemotherapy     Volume:  43     ISSN:  0066-4804     ISO Abbreviation:  Antimicrob. Agents Chemother.     Publication Date:  1999 Apr 
Date Detail:
Created Date:  1999-06-03     Completed Date:  1999-06-03     Revised Date:  2013-06-11    
Medline Journal Info:
Nlm Unique ID:  0315061     Medline TA:  Antimicrob Agents Chemother     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  902-6     Citation Subset:  IM    
Affiliation:
Laboratoire d'Enzymologie, Institut de Chimie, Université de Liège, Belgium.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Anti-Bacterial Agents / metabolism
Bacterial Proteins*
Chelating Agents / pharmacology
Escherichia coli / genetics*,  metabolism
Humans
Hydrogen-Ion Concentration
Kinetics
Picolinic Acids / pharmacology
Pseudomonas aeruginosa / enzymology*
Zinc / metabolism
beta-Lactamases / antagonists & inhibitors,  metabolism*
Chemical
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/Bacterial Proteins; 0/Chelating Agents; 0/Picolinic Acids; 499-83-2/dipicolinic acid; 7440-66-6/Zinc; EC 3.5.2.6/beta-Lactamases
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Structure of In31, a blaIMP-containing Pseudomonas aeruginosa integron phyletically related to In5, ...
Next Document:  Fourteen-member macrolides inhibit interleukin-8 release by human eosinophils from atopic donors.