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Antimicrobial Agents and Chemotherapy, October 2002, p. 3223-3227, Vol. 46, No. 10
0066-4804/02/$04.00+0 DOI: 10.1128/AAC.46.10.3223-3227.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Service de Bactériologie-Virologie, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine Paris-Sud, 94275 Le Kremlin-Bicêtre Cédex, France
Received 7 December 2001/ Returned for modification 24 March 2002/ Accepted 10 July 2002
Empedobacter brevis (formerly designated Flavobacterium breve) is a gram-negative aerobe involved in nosocomial infections. The Ambler class B ß-lactamase gene blaEBR-1 was cloned and expressed in Escherichia coli from E. brevis clinical strain ASS-1, which had reduced susceptibility to expanded-spectrum cephalosporins and carbapenems. Purified ß-lactamase EBR-1 hydrolyzed penicillins, cephalosporins, and carbapenems efficiently but not aztreonam. Kinetic parameters of EBR-1 were similar to those of class B enzymes such as BlaB, IND-2, and GOB-1 identified from other Flavobacteriaceae species, except for meropenem, which was more hydrolyzed by ß-lactamase GOB-1. EBR-1, with a pI of 8.0 and a relative molecular mass of ca. 25 kDa, was classified in functional subgroup 3a, which includes most of the class B ß-lactamases. EBR-1, which belongs to molecular subclass B1 of metalloenzymes, shares 58, 57, and 42% amino acid identity with the most closely related ß-lactamases, IND-1/IND-2 from Chryseobacterium indologenes, CGB-1 from Chryseobacterium gleum, and BlaB from Chryseobacterium meningosepticum, respectively.
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