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Non‐Hydrolytic β‐Lactam Antibiotic Fragmentation by l,d‐Transpeptidases and Serine β‐Lactamase Cysteine Variants

Abstract:

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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Publisher copy:
10.1002/anie.201809424

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Role:
Author
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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:
1433-7851
Pmid:
30569575
Source identifiers:
954401
Language:
English
Keywords:
Pubs id:
pubs:954401
UUID:
uuid:1c5ee022-e6a5-4f45-8f03-1291de0d874b
Local pid:
pubs:954401
Deposit date:
2019-01-08

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