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The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding.

Abstract:

Thiomandelic acid is a simple, broad spectrum, and reasonably potent inhibitor of metallo-beta-lactamases, enzymes that mediate resistance to beta-lactam antibiotics. We report studies by NMR and perturbed angular correlation (PAC) spectroscopy of the mode of binding of the R and S enantiomers of thiomandelic acid, focusing on their interaction with the two metal ions in cadmium-substituted Bacillus cereus metallo-beta-lactamase. The 113Cd resonances are specifically assigned to the metals in...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m301562200

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Journal:
Journal of biological chemistry
Volume:
278
Issue:
31
Pages:
29240-29251
Publication date:
2003-08-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Source identifiers:
38700
Language:
English
Keywords:
Pubs id:
pubs:38700
UUID:
uuid:3728ec8b-e2f9-46ce-b31b-ea2892a54b6e
Local pid:
pubs:38700
Deposit date:
2012-12-19

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