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Titolo:
Inactivation of Aeromonas hydrophila metallo-beta-lactamase by cephamycinsand moxalactam
Autore:
Zervosen, A; Valladares, MH; Devreese, B; Prosperi-Meys, C; Adolph, HW; Mercuri, PS; Vanhove, M; Amicosante, G; van Beeumen, J; Frere, JM; Galleni, M;
Indirizzi:
Univ Liege, Inst Chim B6, Ctr Prot Engn, B-4000 Liege, Belgium Univ LiegeLiege Belgium B-4000 B6, Ctr Prot Engn, B-4000 Liege, Belgium State Univ Ghent, Lab Prot Biochem & Prot Engn, Ghent, Belgium State Univ Ghent Ghent Belgium Prot Biochem & Prot Engn, Ghent, Belgium Univ Saarlandes, Fachrichtung Biochem 8 8, D-6600 Saarbrucken, Germany Univ Saarlandes Saarbrucken Germany D-6600 , D-6600 Saarbrucken, Germany Univ Aquila, Dipartimento Sci & Technol Biomed, I-67100 Laquila, Italy Univ Aquila Laquila Italy I-67100 Technol Biomed, I-67100 Laquila, Italy
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 13, volume: 268, anno: 2001,
pagine: 3840 - 3850
SICI:
0014-2956(200107)268:13<3840:IOAHMB>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
THIOL ESTER DERIVATIVES; ACTIVE-SITE SERINE; BIPHENYL TETRAZOLES; CACODYLIC ACID; INHIBITION; MECHANISM; CARBAPENEMASE; POTENT;
Keywords:
cefoxitin; disulfide bond; inactivation; metallo-beta-lactamase; moxalactam;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Galleni, M Univ Liege, Inst Chim B6, Ctr Prot Engn, B-4000 Liege, Belgium Univ Liege Liege Belgium B-4000 t Engn, B-4000 Liege, Belgium
Citazione:
A. Zervosen et al., "Inactivation of Aeromonas hydrophila metallo-beta-lactamase by cephamycinsand moxalactam", EUR J BIOCH, 268(13), 2001, pp. 3840-3850

Abstract

Incubation of moxalactam and cefoxitin with the Aeromonas hydrophila metallo-beta -lactamase CphA leads to enzyme-catalyzed hydrolysis of both compounds and to irreversible inactivation of the enzyme by the reaction products. As shown by electrospray mass spectrometry, the inactivation of CphA by cefoxitin and moxalactam is accompanied by the formation of stable adducts with mass increases of 445 and 111 Da, respectively. The single thiol group of the inactivated enzyme is no longer titrable, and dithiothreitol treatment of the complexes partially restores the catalytic activity. The mechanism of inactivation by moxalactam was studied in detail. Hydrolysis of moxalactam is followed by elimination of the 3' leaving group (5-mercapto-1-methyltetrazole), which forms a disulfide bond with the cysteine residue of CphAlocated in the active site. Interestingly, this reaction is catalyzed by cacodylate.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 11:02:03