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

Selection of allosteric beta-lactamase mutants featuring an activity regulation by transition metal ions.

Protein science : a publication of the Protein Society - 1 Oct 2006

Mathonet Pascale, Barrios Humberto, Soumillion Patrice, Fastrez Jacques

Abstract excerpt

Libraries of phage-displayed beta-lactamase mutants in which up to three loops have been engineered by genetic introduction of random peptide sequences or by randomization of the wild-type sequence have been submitted to selection protocols designed to find mutants in which binding of transition metal ions to the engineered secondary binding site leads to significant effects on the enzymatic activity. A...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Allosteric Site

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to beta-Lactamases

Share to Copper

Share to Nickel

Share to Peptide Library

Share to Protein Engineering

Source

Open in PubMed Open full text

Identifiers

PMID: 16963642
DOI: 10.1110/ps.062304406
PMCID: PMC2242392

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Selection of allosteric beta-lactamase mutants featuring an activity regulation by transition metal ions.PMID 16963642Read ↗

Engineering allosteric regulation into the hinge region of a circularly permuted TEM-1 beta-lactamase.Semantic proximity Read ↗

A designed supramolecular protein assembly with in vivo enzymatic activity.Semantic proximity Read ↗

Selection of metalloenzymes by catalytic activity using phage display and catalytic elution.Semantic proximity Read ↗

Engineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.Semantic proximity Read ↗

Metallo-β-lactamases: Novel Weaponry for Antibiotic Resistance in BacteriaSemantic proximity Read ↗

Active TEM-1 beta-lactamase mutants with random peptides inserted in three contiguous surface loops.Semantic proximity Read ↗

An altered zinc-binding site confers resistance to a covalent inactivator of New Delhi metallo-beta-lactamase-1 (NDM-1) discovered by high-throughput screening.Semantic proximity Read ↗

The rational design of allosteric interactions in a monomeric protein and its applications to the construction of biosensors.Semantic proximity Read ↗

Targeting the selectivity filter to drastically alter the activity and substrate spectrum of a promiscuous metal transporterSemantic proximity Read ↗

Active-site mutants of class B beta-lactamases: substrate binding and mechanistic study.Semantic proximity Read ↗

Mutational analysis of peptidoglycan amidase MepA.Semantic proximity Read ↗

Probing the role of Met221 in the unusual metallo-β-lactamase GOB-18.Semantic proximity Read ↗

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