AAC
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Docquier, J.-D.
Right arrow Articles by Rossolini, G. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Docquier, J.-D.
Right arrow Articles by Rossolini, G. M.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, December 2004, p. 4778-4783, Vol. 48, No. 12
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.12.4778-4783.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Biochemical Characterization of the THIN-B Metallo-ß-Lactamase of Janthinobacterium lividum

Jean-Denis Docquier,1,{dagger} Teresa Lopizzo,1 Sabrina Liberatori,2 Manuela Prenna,3 Maria Cristina Thaller,4 Jean-Marie Frère,5 and Gian Maria Rossolini1*

Dipartimento di Biologia Molecolare, Laboratorio di Fisiologia e Biotecnologia dei Microrganismi,1 Laboratorio di Proteomica Funzionale, Università di Siena, Siena,2 Dipartimento di Biologia Molecolare, Cellulare e Animale, Università di Camerino, Camerino,3 Dipartimento di Biologia, Università di Roma "Tor Vergata," Rome, Italy,4 Laboratoire d'Enzymologie and Centre d'Ingénierie des Protéines, Institut de Chimie, Université de Liège, Liège, Belgium5

Received 21 January 2004/ Returned for modification 8 May 2004/ Accepted 4 August 2004

The THIN-B metallo-ß-lactamase, a subclass B3 enzyme produced by the environmental species Janthinobacterium lividum, was overproduced in Escherichia coli by means of a T7-based expression system. The enzyme was purified (>95%) by two ion-exchange chromatography steps and subjected to biochemical analysis. The native THIN-B enzyme is a monomeric protein of 31 kDa. It exhibits the highest catalytic efficiencies with carbapenem substrates and cephalosporins, except for cephaloridine, which acts as a poor inactivator. Individual rate constants for inactivation by chelators were measured, suggesting that inactivation occurred by a mechanism involving formation of a ternary complex.

* Corresponding author. Mailing address: Dipartimento di Biologia Molecolare, Università di Siena, Policlinico Le Scotte, 53100 Siena, Italy. Phone: 39 0577 233327. Fax: 39 0577 233325. E-mail: rossolini{at}unisi.it.

{dagger} Present address: Laboratoire d'Enzymologie et Centre d'Ingénierie des Protéines, Institut de Chimie, Université de Liège, B-4000 Liège, Belgium.

Antimicrobial Agents and Chemotherapy, December 2004, p. 4778-4783, Vol. 48, No. 12
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.12.4778-4783.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Clin. Vaccine Immunol. Clin. Microbiol. Rev.
J. Clin. Microbiol. ALL ASM JOURNALS

Copyright © 2004 by the American Society for Microbiology. All rights reserved.