Multiple substitutions at position 104 of beta-lactamase TEM-1: assessing the role of this residue in substrate specificity.

doi:10.1042/bj3050033

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Article

Multiple substitutions at position 104 of beta-lactamase TEM-1: assessing the role of this residue in substrate specificity.

The Biochemical journal - 1 Jan 1995

Petit A, Maveyraud L, Lenfant F, Samama J P, Labia R, Masson J M

Abstract excerpt

Residue 104 is frequently mutated from a glutamic acid to a lysine in the extended-spectrum TEM beta-lactamases responsible for the resistance to third-generation cephalosporins in clinical Gram negative strains. Among class A beta-lactamases, it is the most variable residue within a highly conserved loop which delineates one side of the active site of the enzymes. To investigate the role of this residue in the...

Topics

Amino Acid Sequence
Base Sequence
Binding Sites
Clavulanic Acid
Clavulanic Acids
Enzyme Inhibitors
Escherichia coli
Glutamic Acid
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Conformation

Sequence Homology, Amino Acid

Substrate Specificity

beta-Lactamase Inhibitors

beta-Lactamases

Source

Open in PubMed Open full text

Identifiers

PMID: 7826350
DOI: 10.1042/bj3050033
PMCID: PMC1136426

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7826350-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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