Two non-active site residues W165 and L166 prominently influence the beta-lactam hydrolytic ability of OXA-23 beta-lactamase
Author:
Funder
Department of Biotechnology, Ministry of Science and Technology
Council of Scientific and Industrial Research
Publisher
Springer Science and Business Media LLC
Subject
Drug Discovery,Pharmacology
Link
https://www.nature.com/articles/s41429-023-00624-z.pdf
Reference36 articles.
1. Ambler RP. The structure of beta-lactamases. Philos Trans R Soc Lond B Biol Sci. 1980;289:321–31.
2. Vuillemenot JB, Bour M, Beyrouthy R, Bonnet R, Laaberki MH, Charpentier X, et al. Genomic analysis of CTX-M-115 and OXA-23/-72 co-producing Acinetobacter baumannii, and their potential to spread resistance genes by natural transformation. J Antimicrob Chemother. 2022;77:1542–52.
3. Karthikeyan K, Thirunarayan MA, Krishnan P. Coexistence of bla(OXA-23) with bla(NDM-1) and armA in clinical isolates of Acinetobacter baumannii from India. J Antimicrob Chemother. 2010;65:2253–4.
4. La MV, Jureen R, Lin RTP, Teo JWP. Unusual detection of an acinetobacter class D carbapenemase gene, bla(OXA-23), in a clinical Escherichia coli isolate. J Clin Microbiol. 2014;52:3822–3.
5. Bush K, Jacoby GA. Updated functional classification of beta-lactamases. Antimicrob Agents Chemother. 2010;54:969–76.
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