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Investigations on recyclisation and hydrolysis in avibactam mediated serine β-lactamase inhibition.

Abstract:

β-Lactams inhibit penicillin-binding proteins (PBPs) and serine β-lactamases by acylation of a nucleophilic active site serine. Avibactam is approved for clinical use in combination with ceftazidime, and is a breakthrough non β-lactam β-lactamase inhibitor also reacting via serine acylation. Molecular dynamics (MD) and quantum chemical calculations on avibactam-mediated inhibition of a clinically relevant cephalosporinase reveal that recyclisation of the avibactam derived carbamoyl complex is...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1039/c6ob00353b

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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Grant:
Ministry of Science, ICT and Future Planning (2015M3D1A1069705)
Medical Research Council More from this funder
AstraZeneca More from this funder
Publisher:
Royal Society of Chemistry Publisher's website
Journal:
Organic and Biomolecular Chemistry Journal website
Publication date:
2016
DOI:
EISSN:
1477-0539
ISSN:
1477-0520
URN:
uuid:df77a5ea-789f-4278-be82-d436b80922b3
Source identifiers:
616726
Local pid:
pubs:616726
Language:
English

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