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

Back mutations to the TEM-1 beta-lactamase from TRC-1 lead to restored sensitivity to clavulanic acid.

Journal of medical microbiology - 1 Jun 1995

Thomson C J, Amyes S G

Abstract excerpt

Back mutations from the TRC-1 beta-lactamase to the TEM-1 enzyme were selected in vitro. The revertant beta-lactamase was obtained from Escherichia coli strain J62.2 carrying plasmid pUK901 which encodes the TRC-1 beta-lactamase. The revertant was obtained after repeated subculture of E. coli J62.2 (pUK901) in amoxycillin 512 mg/L for 5 days. The revertant beta-lactamase had the same pI as TEM-1 (5.4) and had...

Topics

Amoxicillin
Anti-Bacterial Agents
Clavulanic Acid
Clavulanic Acids
DNA, Bacterial
Drug Resistance, Microbial
Escherichia coli
Isoelectric Focusing
Mutation
Restriction Mapping
beta-Lactamase Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

beta-Lactamases

Source

Identifiers

PMID: 7791208
DOI: 10.1099/00222615-42-6-429

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7791208-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Back mutations to the TEM-1 beta-lactamase from TRC-1 lead to restored sensitivity to clavulanic acid.PMID 7791208Read ↗

A complex mutant of TEM-1 beta-lactamase with mutations encountered in both IRT-4 and extended-spectrum TEM-15, produced by an Escherichia coli clinical isolate.Semantic proximity Read ↗

In vivo selection of a complex mutant TEM (CMT) from an inhibitor-resistant TEM (IRT) during ceftazidime therapy.Semantic proximity Read ↗

Selection of variants of the TEM-1 beta-lactamase, encoded by a plasmid of clinical origin, with increased resistance to beta-lactamase inhibitors.Semantic proximity Read ↗

A237T as a modulating mutation in naturally occurring extended-spectrum TEM-type beta-lactamases.Semantic proximity Read ↗

TEM-109 (CMT-5), a natural complex mutant of TEM-1 beta-lactamase combining the amino acid substitutions of TEM-6 and TEM-33 (IRT-5).Semantic proximity Read ↗

Co‐production of Tet(X) and MCR ‐1, two resistance enzymes by a single plasmidSemantic proximity Read ↗

A Novel Deletion Mutation in pmrB Contributes to Concurrent Colistin Resistance in Carbapenem-Resistant Escherichia coli Sequence Type 405 of Clinical OriginSemantic proximity Read ↗

Mechanistic Insights into Crosstalk of Tet(X) and MCR-1, Two Resistance Enzymes Co-produced by A Single PlasmidSemantic proximity Read ↗

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