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

Roles of residues Cys69, Asn104, Phe160, Gly232, Ser237, and Asp240 in extended-spectrum beta-lactamase Toho-1.

Antimicrobial agents and chemotherapy - 1 Jan 2011

Shimizu-Ibuka Akiko, Oishi Mika, Yamada Shoko, Ishii Yoshikazu, Mura Kiyoshi, Sakai Hiroshi, Matsuzawa Hiroshi

Abstract excerpt

Toho-1, which is also designated CTX-M-44, is an extended-spectrum class A β-lactamase that has high activity toward cefotaxime. In this study, we investigated the roles of residues suggested to be critical for the substrate specificity expansion of Toho-1 in previous structural analyses. Six amino acid residues were replaced one by one with amino acids that are often observed in the corresponding position of...

Read the complete abstract on PubMed

Topics

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

Share to Anti-Bacterial Agents
Share to beta-Lactamases

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

Share to Cefotaxime

Share to Microbial Sensitivity Tests

Share to Mutagenesis, Site-Directed

Share to Sequence Homology, Amino Acid

Share to Structure-Activity Relationship

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 21078949
DOI: 10.1128/AAC.00098-10
PMCID: PMC3019690

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

Roles of residues Cys69, Asn104, Phe160, Gly232, Ser237, and Asp240 in extended-spectrum beta-lactamase Toho-1.PMID 21078949Read ↗

Detailed investigation of catalytically important residues of class A β-lactamaseSemantic proximity Read ↗

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

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

Characterization of the global stabilizing substitution A77V and its role in the evolution of CTX-M β-lactamases.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 ↗

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 ↗

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

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

Effect of an amino acid insertion into the omega loop region of a class C beta-lactamase on its substrate specificity.Semantic proximity Read ↗

Comprehensive exploration of the translocation, stability and substrate recognition requirements in VIM-2 lactamaseSemantic proximity Read ↗

Comprehensive exploration of the translocation, stability and substrate recognition requirements in VIM-2 lactamase.Semantic proximity Read ↗

Role of a mutation at position 167 of CTX-M-19 in ceftazidime hydrolysis.Semantic proximity Read ↗

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