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 lead to increased loop flexibility and expanded specificity in Acinetobacter baumannii carbapenemase OXA-239.

The Biochemical journal - 11 Jan 2018

Harper Thomas M, June Cynthia M, Taracila Magdalena A, Bonomo Robert A, Powers Rachel A, Leonard David A

Abstract excerpt

OXA-239 is a class D carbapenemase isolated from an Acinetobacter baumannii strain found in Mexico. This enzyme is a variant of OXA-23 with three amino acid substitutions in or near the active site. These substitutions cause OXA-239 to hydrolyze late-generation cephalosporins and the monobactam aztreonam with greater efficiency than OXA-23. OXA-239 activity against the carbapenems doripenem and imipenem is...

Read the complete abstract on PubMed

Topics

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

Share to Acinetobacter baumannii
Share to beta-Lactamases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Carbapenems

Share to Cefotaxime

Share to Imipenem

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Source

Open in PubMed Open full text

Identifiers

PMID: 29229762
DOI: 10.1042/BCJ20170702
PMCID: PMC5988212

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

Multiple substitutions lead to increased loop flexibility and expanded specificity in Acinetobacter baumannii carbapenemase OXA-239.PMID 29229762Read ↗

The structure of a doripenem‐bound OXA‐51 class D β‐lactamase variant with enhanced carbapenemase activitySemantic proximity Read ↗

Structures of the Class D Carbapenemases OXA-23 and OXA-146: Mechanistic Basis of Activity against Carbapenems, Extended-Spectrum Cephalosporins, and AztreonamSemantic proximity Read ↗

Crystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysisSemantic proximity Read ↗

Exploring the Role of the Ω-Loop in the Evolution of Ceftazidime Resistance in the PenA β-Lactamase from Burkholderia multivorans, an Important Cystic Fibrosis PathogenSemantic proximity Read ↗

Clinical Variants of the Native Class D β-Lactamase of Acinetobacter baumannii Pose an Emerging Threat through Increased Hydrolytic Activity against CarbapenemsSemantic proximity Read ↗

Expanded Substrate Activity of OXA-24/40 in Carbapenem-Resistant Acinetobacter baumannii Involves Enhanced Binding Loop Flexibility.Semantic proximity Read ↗

Structural Basis for Enhancement of Carbapenemase Activity in the OXA-51 Family of Class D β-LactamasesSemantic proximity Read ↗

Complementary roles of mutations at positions 69 and 242 in a class A beta-lactamase.Semantic proximity Read ↗

C6 Hydroxymethyl-Substituted Carbapenem MA-1-206 Inhibits the Major Acinetobacter baumannii Carbapenemase OXA-23 by Impeding DeacylationSemantic 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 ↗

Construction and characterization of an OHIO-1 beta-lactamase bearing Met69Ile and Gly238Ser mutations.Semantic proximity Read ↗

Klebsiella pneumoniae Carbapenemase-2 (KPC-2), Substitutions at Ambler Position Asp179, and Resistance to Ceftazidime-Avibactam: Unique Antibiotic-Resistant Phenotypes Emerge from β-Lactamase Protein Engineering.Semantic proximity Read ↗

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