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Article

Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamase.

Protein science : a publication of the Protein Society - 1 Oct 2009

Marciano David C, Brown Nicholas G, Palzkill Timothy

Abstract excerpt

A large number of beta-lactamases have emerged that are capable of conferring bacterial resistance to beta-lactam antibiotics. Comparison of the structural and functional features of this family has refined understanding of the catalytic properties of these enzymes. An arginine residue present at position 244 in TEM-1 beta-lactamase interacts with the carboxyl group common to penicillin and cephalosporin...

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Identifiers

PMID: 19672877
DOI: 10.1002/pro.220
PMCID: PMC2786972

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamase.PMID 19672877Read ↗

Exploring the coupling of dynamic residues in TEM-1 β-lactamase and their role in activity.Semantic proximity Read ↗

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Unveiling the evolution routes of TEM-type extended-spectrum β-lactamases.Semantic proximity Read ↗

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Phenotypic study of resistance of beta-lactamase-inhibitor-resistant TEM enzymes which differ by naturally occurring variations and by site-directed substitution at Asp276.Semantic proximity Read ↗

Capturing the mutational landscape of the beta-lactamase TEM-1.Semantic proximity Read ↗

Overall mutational scanning unveils the essential active residues for the mechanistic action of MCR-1.Semantic proximity Read ↗

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Complementary roles of mutations at positions 69 and 242 in a class A beta-lactamase.Semantic proximity Read ↗

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