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The role of active site flexible loops in catalysis and of zinc in conformational stability of Bacillus cereus 569/H/9 β-lactamase.

Abstract:

Metallo-β-lactamases catalyse the hydrolysis of most β-lactam antibiotics and hence represent a major clinical concern. The development of inhibitors for these enzymes is complicated by the diversity and flexibility of their substrate binding sites, motivating research into their structure and function. In this study, we examined the conformational properties of the Bacillus cereus β-lactamase II in the presence of chemical denaturants using a variety of...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted manuscript

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Publisher copy:
10.1074/jbc.M116.719005

Authors


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National Fund for Scientific Research More from this funder
Publisher:
American Society for Biochemistry and Molecular Biology Publisher's website
Journal:
The Journal of Biological Chemistry Journal website
Pages:
jbc.M116.719005
Publication date:
2016-05-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:31f383f9-62ac-4276-9650-8708862fb452
Source identifiers:
625255
Local pid:
pubs:625255

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