Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Base Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Binding Sites

Share to Escherichia coli

Share to Kinetics

Share to Molecular Sequence Data

Share to Mutation

Share to Sequence Homology, Amino Acid

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 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multiple substitutions at position 104 of beta-lactamase TEM-1: assessing the role of this residue in substrate specificity.PMID 7826350Read ↗

Distant and new mutations in CTX-M-1 beta-lactamase affect cefotaxime hydrolysis.Semantic proximity Read ↗

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

Mutation of the conserved Asp-Asp pair impairs the structure, function, and inhibition of CTX-M Class A β-lactamase.Semantic proximity Read ↗

Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution.Semantic proximity Read ↗

High tolerance to simultaneous active-site mutations in TEM-1 beta-lactamase: Distinct mutational paths provide more generalized beta-lactam recognition.Semantic proximity Read ↗

[Bacterial TEM-type serine beta-lactamases: structure and analysis of mutations].Semantic proximity Read ↗

A drug-resistant β-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency.Semantic proximity Read ↗

Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase.Semantic proximity Read ↗

A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis.Semantic proximity Read ↗

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 ↗

Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 beta-lactamase with beta-lactamase inhibitory protein.Semantic proximity Read ↗

Variants of subtilisin BPN' with altered specificity profiles.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.