Thiomandelic Acid, a Broad Spectrum Inhibitor of Zinc β-Lactamases: KINETIC AND SPECTROSCOPIC STUDIES* 210

C Mollard, C Moali, C Papamicael, C Damblon… - Journal of Biological …, 2001 - ASBMB
Resistance to β-lactam antibiotics mediated by metallo-β-lactamases is an increasingly
worrying clinical problem. Candidate inhibitors include mercaptocarboxylic acids, and we …

Inhibitors of metallo-β-lactamase generated from β-lactam antibiotics

A Badarau, A Llinás, AP Laws, C Damblon… - Biochemistry, 2005 - ACS Publications
The resistance of bacteria to the normally lethal action of β-lactam antibiotics is largely due
to the production of β-lactamases that catalyze the hydrolysis of the β-lactam. One class of …

Inhibition of metallo-β-lactamases by a series of thiol ester derivatives of mercaptophenylacetic acid

DJ Payne, JH Bateson, BC Gasson… - FEMS microbiology …, 1997 - academic.oup.com
A series of mercaptophenylacetic acid thiol esters bearing a phenyl substituent adjacent to
the carboxylic acid function has been shown to be inhibitors of metallo-β-lactamases. The …

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

C Damblon, M Jensen, A Ababou, I Barsukov… - Journal of Biological …, 2003 - ASBMB
Thiomandelic acid is a simple, broad spectrum, and reasonably potent inhibitor of metallo-β-
lactamases, enzymes that mediate resistance to β-lactam antibiotics. We report studies by …

Inhibition of metallo-beta-lactamases by a series of mercaptoacetic acid thiol ester derivatives

DJ Payne, JH Bateson, BC Gasson… - Antimicrobial agents …, 1997 - Am Soc Microbiol
A series of mercaptoacetic acid thiol esters have been identified as metallo-beta-lactamase
inhibitors. Electrospray mass spectrometry (ESMS) has shown that irreversible inhibition of …

Histidine residues of zinc ligands in β-lactamase II

GS Baldwin, A Galdes, HAO Hill, BE Smith… - Biochemical …, 1978 - portlandpress.com
1. The Zn (II)-requiring beta-lactamase from Bacillus cereus 569/H/9, which has two zinc-
binding sites, was examined by 270 MHz 1H nmr spectroscopy. Resonances were assigned …

Zinc-bound thiolate− disulfide exchange: a strategy for inhibiting metallo-β-lactamases

H Boerzel, M Koeckert, W Bu, B Spingler… - Inorganic …, 2003 - ACS Publications
The mononuclear zinc thiolate complexes [(TpPhMe) Zn (SR)], where TpPhMe is hydrotris
((3-methyl-5-phenyl) pyrazolyl) borate and (SR) is benzyl thiolate, 4-nitrophenylthiolate, 4 …

Unanticipated Inhibition of the Metallo-β-lactamase from Bacteroides fragilis by 4-Morpholineethanesulfonic Acid (MES):  A Crystallographic Study at 1.85-Å …

PMD Fitzgerald, JK Wu, JH Toney - Biochemistry, 1998 - ACS Publications
As part of a structure-aided effort to design clinically useful inhibitors of metallo-β-
lactamases, the X-ray crystal structure of a complex between the metallo-β-lactamase from …

The mechanism of catalysis and the inhibition of β-lactamases

MI Page, AP Laws - Chemical Communications, 1998 - pubs.rsc.org
Formation of a tetrahedral intermediate by nucleophilic attack on the β-lactam carbonyl
carbon of penicillins generates a lone pair on the β-lactam nitrogen which is syn to the …

The inhibition of metallo-β-lactamase by thioxo-cephalosporin derivatives

WY Tsang, A Dhanda, CJ Schofield, JM Frère… - Bioorganic & medicinal …, 2004 - Elsevier
The 8-thioxocephalosporins are poor substrates for the B. cereus metallo β-lactamase
(kcat/Km= 61.4 M− 1 s− 1) and act as weak competitive inhibitors (Ki∼ 700 μM). The …