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Inhibition of TEM-2 beta-lactamase from Escherichia coli by clavulanic acid: observation of intermediates by electrospray ionization mass spectrometry.

Abstract:

Clavulanic acid, the therapeutically important inhibitor of beta-lactamases containing a nucleophilic serine residue at their active sites, inhibits Escherichia coli TEM-2 beta-lactamase via a complex mechanism. Electrospray ionization mass spectrometry (ESIMS) studies revealed that a minimum of four different modified proteins are formed upon incubation of clavulanate with the TEM-2 enzyme. These exhibit mass increments relative to the unmodified TEM-2 beta-lactamase of 52, 70, 88, and 155 D...

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Publication status:
Published

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Publisher copy:
10.1021/bi961044g

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Journal:
Biochemistry
Volume:
35
Issue:
38
Pages:
12421-12432
Publication date:
1996-09-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:ac33dbf3-f8a5-4aee-bc58-ee86df60183c
Source identifiers:
35977
Local pid:
pubs:35977

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