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

Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release.

The Journal of biological chemistry - 4 Feb 2005

Eschenburg Susanne, Priestman Melanie, Schönbrunn Ernst

Abstract excerpt

MurA (UDP-N-acetylglucosamine enolpyruvyl transferase, EC 2.5.1.7) is an essential enzyme in the biosynthesis of the peptidoglycan layer of the bacterial cell. It provides an attractive template for the design of novel antibiotic drugs and is the target of the naturally occurring antibiotic fosfomycin, which covalently attaches to Cys115 in the active site of the enzyme. Mutations of Cys115 to Asp exist in...

Read the complete abstract on PubMed

Topics

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

Share to Alkyl and Aryl Transferases
Share to Anti-Bacterial Agents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to Crystallography

Share to Cystine

Share to Enterobacter cloacae

Share to Fosfomycin

Share to Protein Structure, Tertiary

Source

Identifiers

PMID: 15531591
DOI: 10.1074/jbc.M411325200

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release.PMID 15531591Read ↗

Lyme disease enolpyruvyl-UDP-GlcNAc synthase: fosfomycin-resistant MurA from Borrelia burgdorferi, a fosfomycin-sensitive mutant, and the catalytic role of the active site Asp.Semantic proximity Read ↗

A large displacement of the SXN motif of Cys115-modified penicillin-binding protein 5 from Escherichia coli.Semantic proximity Read ↗

Differential antibacterial properties of the MurA inhibitors terreic acid and fosfomycin.Semantic proximity Read ↗

Structure-based modelling and dynamics of MurM, a <i>Streptococcus pneumoniae</i> penicillin resistance determinant that functions at the cytoplasmic membrane interfaceSemantic proximity Read ↗

MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis.Semantic proximity Read ↗

Structural and functional characterization of VanG D-Ala:D-Ser ligase associated with vancomycin resistance in Enterococcus faecalis.Semantic proximity Read ↗

Conformational Control of UDP-Galactopyranose Mutase Inhibition.Semantic proximity Read ↗

In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction.Semantic proximity Read ↗

Mutational analysis of active-site residues of the enterococcal D-ala-D-Ala dipeptidase VanX and comparison with Escherichia coli D-ala-D-Ala ligase and D-ala-D-Ala carboxypeptidase VanY.Semantic proximity Read ↗

Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism.Semantic proximity Read ↗

Reactivity of asparagine residue at the active site of the D105N mutant of fluoroacetate dehalogenase from Moraxella sp. B.Semantic proximity Read ↗

Scintillation proximity assay for inhibitors of Escherichia coli MurG and, optionally, MraY.Semantic proximity Read ↗

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