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Titolo:
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase
Autore:
Bounaga, S; Galleni, M; Laws, AP; Page, MI;
Indirizzi:
Univ Huddersfield, Dept Chem & Biol Sci, Huddersfield HD1 3DH, W Yorkshire, England Univ Huddersfield Huddersfield W Yorkshire England HD1 3DH shire, England Univ Liege, Ctr Ingn Prot, Inst Chim B6, B-4000 Liege 1, Belgium Univ Liege Liege Belgium 1 n Prot, Inst Chim B6, B-4000 Liege 1, Belgium
Titolo Testata:
BIOORGANIC & MEDICINAL CHEMISTRY
fascicolo: 2, volume: 9, anno: 2001,
pagine: 503 - 510
SICI:
0968-0896(200102)9:2<503:CPIOBC>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
THIOL ESTER DERIVATIVES; BACTEROIDES-FRAGILIS; CRYSTAL-STRUCTURE; STENOTROPHOMONAS-MALTOPHILIA; ANGSTROM RESOLUTION; BIPHENYL TETRAZOLES; ACTIVE-SITE; GENE; AEROMONAS; MECHANISM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Page, MI Univ Huddersfield, Dept Chem & Biol Sci, Huddersfield HD1 3DH, W Yorkshire, England Univ Huddersfield Huddersfield W Yorkshire England HD1 3DH gland
Citazione:
S. Bounaga et al., "Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase", BIO MED CH, 9(2), 2001, pp. 503-510

Abstract

Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-beta -lactamase. The pH dependence of pK(i) indicates that the thiol anion displaces hydroxideion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 21:45:00