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Distant Site Mutations in Clinical TEM Beta-Lactamase Variants Enhance Non-Covalent Binding to Ceftazidime: Insights from Spectroscopic and Biophysical Investigations

2025-08-06

Abstract excerpt

β-lactamases retain the central armamentarium against the β-lactams, resulting in surge of antibiotic resistance, primarily due to the hydrolysis of the amide bond of the four-membered ring. This study aimed to investigate the binding interactions of ceftazidime (CAZ) to TEM β- lactamase variants with distant site mutations isolated from clinical setting to explore the cause of their selection and dissemination du...

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Literature Corpus work
acf37b93-0833-541b-afc0-1326986a4507
DOI
10.1101/2025.08.06.661929
Open publication

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Distant Site Mutations in Clinical TEM Beta-Lactamase Variants Enhance Non-Covalent Binding to Ceftazidime: Insights from Spectroscopic and Biophysical InvestigationsDOI 10.1101/2025.08.06.661929
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