Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase

Sakina Bounaga; Moreno Galleni; Andrew P. Laws; Michael I. Page

doi:10.1016/S0968-0896(00)00257-1

Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase

Sakina Bounaga, Moreno Galleni, Andrew P. Laws, Michael I. Page

University of Liege

Research output: Contribution to journal › Article › peer-review

58 Citations (Scopus)

Abstract

Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-lactamase. The pH dependence of pK_i indicates that the thiol anion displaces hydroxide ion 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.

Original language	English
Pages (from-to)	503-510
Number of pages	8
Journal	Bioorganic and Medicinal Chemistry
Volume	9
Issue number	2
DOIs	https://doi.org/10.1016/S0968-0896(00)00257-1
Publication status	Published - Feb 2001

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title = "Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase",

abstract = "Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion 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.",

author = "Sakina Bounaga and Moreno Galleni and Laws, \{Andrew P.\} and Page, \{Michael I.\}",

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AU - Bounaga, Sakina

AU - Galleni, Moreno

AU - Laws, Andrew P.

AU - Page, Michael I.

PY - 2001/2

Y1 - 2001/2

N2 - Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion 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.

AB - Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion 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.

UR - https://www.scopus.com/pages/publications/0035078014

U2 - 10.1016/S0968-0896(00)00257-1

DO - 10.1016/S0968-0896(00)00257-1

M3 - Article

C2 - 11249142

AN - SCOPUS:0035078014

SN - 0968-0896

VL - 9

SP - 503

EP - 510

JO - Bioorganic and Medicinal Chemistry

JF - Bioorganic and Medicinal Chemistry

IS - 2

ER -

Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase

Abstract

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