Journal article
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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Authors
Funding
Department of Health, Australian Government | National Health and Medical Research Council
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Bibliographic Details
- Publisher:
- American Society for Microbiology Publisher's website
- Journal:
- Antimicrobial Agents and Chemotherapy Journal website
- 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
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
1188244
- Local pid:
- pubs:1188244
- Deposit date:
- 2021-10-12
Terms of use
- Copyright holder:
- American Society for Microbiology
- Copyright date:
- 2021
- Rights statement:
- © 2021 American Society for Microbiology. All Rights Reserved.
- Notes:
-
This is the accepted manuscript version of the article. The final version is available from American Society for Microbiology at https://doi.org/10.1128/AAC.00936-21
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