Journal article
Non‐Hydrolytic β‐Lactam Antibiotic Fragmentation by l,d‐Transpeptidases and Serine β‐Lactamase Cysteine Variants
- Abstract:
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Enzymes often use nucleophilic serine, threonine, and cysteine residues to achieve the same type of reaction; the underlying reasons for this are not understood. While bacterial d,d‐transpeptidases (penicillin‐binding proteins) employ a nucleophilic serine, l,d‐transpeptidases use a nucleophilic cysteine. The covalent complexes formed by l,d‐transpeptidases with some β‐lactam antibiotics undergo non‐hydrolytic fragmentation. This is not usually observed for penicillin‐binding proteins, or for...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, pdf, 2.5MB)
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- Publisher copy:
- 10.1002/anie.201809424
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Authors
Funding
Bibliographic Details
- Publisher:
- Wiley Publisher's website
- Journal:
- Angewandte Chemie International Edition Journal website
- Volume:
- 58
- Issue:
- 7
- Pages:
- 1990-1994
- Publication date:
- 2018-12-20
- Acceptance date:
- 2018-12-19
- DOI:
- EISSN:
-
1521-3773
- ISSN:
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1433-7851
- Pmid:
-
30569575
- Source identifiers:
-
954401
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:954401
- UUID:
-
uuid:1c5ee022-e6a5-4f45-8f03-1291de0d874b
- Local pid:
- pubs:954401
- Deposit date:
- 2019-01-08
Terms of use
- Copyright holder:
- Wiley
- Copyright date:
- 2018
- Notes:
- © 2019 The Authors. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Licence:
- CC Attribution (CC BY)
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