Purification and biochemical characterization of IMP-13 metallo-β-lactamase

[en] The IMP-13 metallo-β-lactamase was overproduced in Escherichia coli BL21(DE3) and purified by chromatography. Analysis of kinetic parameters revealed some notable differences with other IMP-type enzymes, noteworthily a higher catalytic efficiency toward ticarcillin and piperacillin and a marked preference for imipenem over meropenem. Copyright © 2011 American Society for Microbiology. All Rights Reserved.

Disciplines :

Biochemistry, biophysics & molecular biology
Microbiology

Author, co-author :

Santella, G.; Cátedra de Microbiología, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín 956, CP 1113 Buenos Aires, Argentina

Docquier, Jean-Denis ; Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines

Gutkind, G.; Cátedra de Microbiología, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín 956, CP 1113 Buenos Aires, Argentina

Rossolini, G. M.; Dipartimento di Biologia Molecolare, Laboratorio di Fisiologia e Biotecnologie dei Microrganismi, Universita di Siena, I-53100 Siena, Italy

Radice, M.; Cátedra de Microbiología, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín 956, CP 1113 Buenos Aires, Argentina

Language :

English

Title :

Purification and biochemical characterization of IMP-13 metallo-β-lactamase

Publication date :

2011

Journal title :

Antimicrobial Agents and Chemotherapy

ISSN :

0066-4804

eISSN :

1098-6596

Publisher :

American Society for Microbiology, Washington, United States - District of Columbia

Volume :

Issue :

Pages :

399-401

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 20 November 2020

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Bibliography

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