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Titolo:
Biochemical characterization of the FEZ-1 metallo-alpha-lactamase of Legionella gormanii ATCC 33297(T) produced in Escherichia coli
Autore:
Mercuri, PS; Bouillenne, F; Boschi, L; Lamote-Brasseur, J; Amicosante, G; Devreese, B; Van Beeumen, J; Frere, JM; Rossolini, GM; Galleni, M;
Indirizzi:
Univ Liege, Ctr Ingn Prot, B-4000 Liege, Belgium Univ Liege Liege Belgium B-4000 ge, Ctr Ingn Prot, B-4000 Liege, Belgium State Univ Ghent, Lab Eitwitbiochem Eiwitengn, B-9000 Ghent, Belgium StateUniv Ghent Ghent Belgium B-9000 m Eiwitengn, B-9000 Ghent, Belgium Univ Siena, Dipartimento Biol Mol, Sez Microbiol, I-53100 Siena, Italy Univ Siena Siena Italy I-53100 Mol, Sez Microbiol, I-53100 Siena, Italy Univ Aquila, Dipartimento Sci & Tecnol Biomed, I-67100 Coppito, Laquila, Italy Univ Aquila Coppito Laquila Italy I-67100 I-67100 Coppito, Laquila, Italy
Titolo Testata:
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
fascicolo: 4, volume: 45, anno: 2001,
pagine: 1254 - 1262
SICI:
0066-4804(200104)45:4<1254:BCOTFM>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-FRAGILIS TAL3636; HYDROLYZING BETA-LACTAMASES; BACILLUS-CEREUS; CRYSTAL-STRUCTURE; STENOTROPHOMONAS-MALTOPHILIA; PSEUDOMONAS-AERUGINOSA; AEROMONAS-HYDROPHILA; ANGSTROM RESOLUTION; CLINICAL ISOLATE; GENE CASSETTES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Galleni, M Univ Liege, Ctr Ingn Prot, B6 Sart Tilman, B-4000 Liege, Belgium Univ Liege B6 Sart Tilman Liege Belgium B-4000 Liege, Belgium
Citazione:
P.S. Mercuri et al., "Biochemical characterization of the FEZ-1 metallo-alpha-lactamase of Legionella gormanii ATCC 33297(T) produced in Escherichia coli", ANTIM AG CH, 45(4), 2001, pp. 1254-1262

Abstract

The bla(FEZ-1) gene coding for the metallo-beta -lactamase of Legionella (Fluoribacter) gormanii ATCC 33297(T) was overexpressed via a T7 expression system in Escherichia coli BL21(DE3)(pLysS), The product was purified to homogeneity in two steps with a yield of 53%. The FEZ-1 metallo-beta -lactamase exhibited a broad-spectrum activity profile, with a preference for cephalosporins such as cephalothin, cefuroxime, and cefotaxime, Monobactams werenot hydrolyzed, The beta -lactamase was inhibited by metal chelators, FEZ-1 is a monomeric enzyme with a molecular mass of 29,440 Da which possesses two zinc-binding sites. Its zinc content did not vary in the pH range of 5 to 9, but the presence of zinc ions modified the catalytic efficiency of the enzyme. A model of the FEZ-1 three-dimensional structure was built.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 19:28:01