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

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

Molecular microbiology - 1 May 2006

Kim Jae Young, Jung Ha Il, An Young Jun, Lee Jung Hun, Kim So Jung, Jeong Seok Hoon, Lee Kye Joon, Suh Pann-Ghill, Lee Heung-Soo, Lee Sang Hee, Cha Sun-Shin

Abstract excerpt

The emergence and dissemination of extended-spectrum (ES) beta-lactamases induce therapeutic failure and a lack of eradication of clinical isolates even by third-generation beta-lactam antibiotics like ceftazidime. CMY-10 is a plasmid-encoded class C beta-lactamase with a wide spectrum of substrates. Unlike the well-studied class C ES beta-lactamase from Enterobacter cloacae GC1, the Omega-loop does not affect...

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 Crystallography, X-Ray

Share to Enterobacter cloacae

Share to Hydrolysis

Share to Imipenem

Share to Sequence Deletion

Share to Substrate Specificity

Source

Identifiers

PMID: 16677302
DOI: 10.1111/j.1365-2958.2006.05146.x

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

Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase.PMID 16677302Read ↗

High adaptability of the omega loop underlies the substrate-spectrum-extension evolution of a class A β-lactamase, PenL.Semantic proximity Read ↗

Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure.Semantic proximity Read ↗

Characterization of the new AmpC β-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 loop that affects ceftazidime hydrolysis.Semantic proximity Read ↗

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

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

Structure of the extended-spectrum class C beta-lactamase of Enterobacter cloacae GC1, a natural mutant with a tandem tripeptide insertion.Semantic proximity Read ↗

Extension of the hydrolysis spectrum of AmpC beta-lactamase of Escherichia coli due to amino acid insertion in the H-10 helix.Semantic proximity Read ↗

The tandem repeats enabling reversible switching between the two phases of β-lactamase substrate spectrum.Semantic proximity Read ↗

Structural insights into the molecular mechanism of high-level ceftazidime–avibactam resistance conferred by CMY-185Semantic 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 ↗

A Novel CMY Variant Confers Transferable High-Level Resistance to Ceftazidime-Avibactam in Multidrug-Resistant EscherichiacoliSemantic proximity Read ↗

Molecular evolution of ubiquitous beta-lactamases towards extended-spectrum enzymes active against newer beta-lactam antibiotics.Semantic proximity Read ↗

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