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

Streptococcal dTDP‐L‐rhamnose biosynthesis enzymes: functional characterization and lead compound identification

2 Jan 2019

Abstract excerpt

Summary Biosynthesis of the nucleotide sugar precursor dTDP‐L‐rhamnose is critical for the viability and virulence of many human pathogenic bacteria, including Streptococcus pyogenes (Group A Streptococcus ; GAS), Streptococcus mutans and Mycobacterium tuberculosis . Streptococcal pathogens require dTDP‐L‐rhamnose for the production of structurally similar rhamnose polysaccharides in their cell wall. Via...

Read the complete abstract on PubMed

Topics

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

Share to Diet, Metabolism, and Disease
Share to Enzyme Structure and Function
Share to Genomics and Phylogenetic Studies

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 30600561
DOI: 10.1111/mmi.14197

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Streptococcal dTDP‐L‐rhamnose biosynthesis enzymes: functional characterization and lead compound identificationPMID 30600561Read ↗

Streptococcal dTDP-L-rhamnose biosynthesis enzymes: functional characterization and lead compound identificationSemantic proximity Read ↗

A structural perspective on the enzymes that convert dTDP-d-glucose into dTDP-l-rhamnoseSemantic proximity Read ↗

Rhamnose-Containing Compounds: Biosynthesis and ApplicationsSemantic proximity Read ↗

Disruption of l-Rhamnose Biosynthesis Results in Severe Growth Defects in Streptococcus mutans.Semantic proximity Read ↗

Bacterial glycobiology: rhamnose-containing cell wall polysaccharides in Gram-positive bacteriaSemantic proximity Read ↗

Insights into the central role of N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) in peptidoglycan metabolism and its potential as a therapeutic targetSemantic proximity Read ↗

GacA is essential for Group A Streptococcus and defines a new class of monomeric dTDP-4-dehydrorhamnose reductases (RmlD).Semantic proximity Read ↗

Characterization of dTDP-4-dehydrorhamnose 3,5-Epimerase and dTDP-4-dehydrorhamnose Reductase, Required for dTDP-l-rhamnose Biosynthesis in Salmonella enterica Serovar Typhimurium LT2Semantic proximity Read ↗

Novel dTDP-l-Rhamnose Synthetic Enzymes (RmlABCD) From Saccharothrix syringae CGMCC 4.1716 for One-Pot Four-Enzyme Synthesis of dTDP-l-RhamnoseSemantic proximity Read ↗

Discovery of glycerol phosphate modification on streptococcal rhamnose polysaccharidesSemantic proximity Read ↗

An Optimized Marinopyrrole A Derivative Targets 6-Phosphoglucosamine Synthetase to Inhibit Methicillin-Resistant Staphylococcus aureusSemantic proximity Read ↗

Discovery of glycerol phosphate modification on streptococcal rhamnose polysaccharidesSemantic proximity Read ↗

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