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Kinetic and structural characterization of the first B3 metallo-β-lactamase with an active-site glutamic acid

Abstract:

The structural diversity in metallo-β-lactamases (MBLs), especially in the vicinity of the active site, has been a major hurdle in the development of clinically effective inhibitors. Representatives from three variants of the B3 MBL subclass, containing either the canonical HHH/DHH active-site motif (present in the majority of MBLs in this subclass) or the QHH/DHH (B3-Q) or HRH/DQK (B3-RQK) variations, were reported previously. Here, we describe the structure and kinetic properties of the fir...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1128/aac.00936-21

Authors


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Role:
Author
ORCID:
0000-0002-4439-7738
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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
ORCID:
0000-0002-0290-6565
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Name:
Department of Health, Australian Government | National Health and Medical Research Council
Publisher:
American Society for Microbiology
Journal:
Antimicrobial Agents and Chemotherapy More from this journal
Volume:
65
Issue:
10
Article number:
e0093621
Publication date:
2021-07-26
Acceptance date:
2021-07-19
DOI:
EISSN:
1098-6596
ISSN:
0066-4804
Pmid:
34310207
Language:
English
Keywords:
Pubs id:
1188244
Local pid:
pubs:1188244
Deposit date:
2021-10-12

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