ArticleEMBO reports2008
A structural basis for the allosteric regulation of non-hydrolysing UDP-GlcNAc 2-epimerases.
Article in EMBO reports, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 40 citations in OpenAlex.
- Insights into structure and activity of a UDP-GlcNAc 2-epimerase involved in secondary cell wall polymer biosynthesis inFrontiers in molecular biosciences · 2024Article
- Structural analysis of a bacterial UDP-sugar 2-epimerase reveals the active site architecture before and after catalysis.The Journal of biological chemistry · 2023Article
- PAC-FragmentDEL - photoactivated covalent capture of DNA-encoded fragments for hit discovery.RSC medicinal chemistry · 2022Article
- Protein kinase inhibitor ceritinib blocks ectonucleotidase CD39 - a promising target for cancer immunotherapy.Journal for immunotherapy of cancer · 2022Article
- Article
- Structural characterization of a nonhydrolyzing UDP-GlcNAc 2-epimerase from Neisseria meningitidis serogroup A.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Extracellular polysaccharide synthesis in a bloom-forming strain of Microcystis aeruginosa: implications for colonization and buoyancy.Scientific reports · 2019Article
- Review
- Substrate-Dependence of Competitive Nucleotide Pyrophosphatase/Phosphodiesterase1 (NPP1) Inhibitors.Frontiers in pharmacology · 2017Article
- CovR Regulates Streptococcus mutans Susceptibility To Complement Immunity and Survival in Blood.Infection and immunity · 2016Article
- Chemical Genetic Analysis and Functional Characterization of Staphylococcal Wall Teichoic Acid 2-Epimerases Reveals Unconventional Antibiotic Drug Targets.PLoS pathogens · 2016Article
- Mechanism and inhibition of human UDP-GlcNAc 2-epimerase, the key enzyme in sialic acid biosynthesis.Scientific reports · 2016Article
- Characterizing non-hydrolyzing Neisseria meningitidis serogroup A UDP-N-acetylglucosamine (UDP-GlcNAc) 2-epimerase using UDP-N-acetylmannosamine (UDP-ManNAc) and derivatives.Carbohydrate research · 2016Article
- Bacillus anthracis lcp Genes Support Vegetative Growth, Envelope Assembly, and Spore Formation.Journal of bacteriology · 2015Article
- Bacillus anthracis tagO Is Required for Vegetative Growth and Secondary Cell Wall Polysaccharide Synthesis.Journal of bacteriology · 2015Article
- Structural and enzymatic analysis of TarM glycosyltransferase from Staphylococcus aureus reveals an oligomeric protein specific for the glycosylation of wall teichoic acid.The Journal of biological chemistry · 2015Article
- A novel polyamine allosteric site of SpeG from Vibrio cholerae is revealed by its dodecameric structure.Journal of molecular biology · 2015Article
- GneZ, a UDP-GlcNAc 2-epimerase, is required for S-layer assembly and vegetative growth of Bacillus anthracis.Journal of bacteriology · 2014Article
- Use of a bacteriophage lysin to identify a novel target for antimicrobial development.PloS one · 2013Article
- The structural biology of enzymes involved in natural product glycosylation.Natural product reports · 2012Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The non-hydrolysing bacterial UDP-N-acetylglucosamine 2-epimerase (UDP-GlcNAc 2-epimerase) catalyses the conversion of UDP-GlcNAc into UDP-N-acetylmannosamine, an intermediate in the biosynthesis of several cell-surface polysaccharides. This enzyme is allosterically regulated by its substrate UDP-GlcNAc. The structure of the ternary complex between the Bacillus anthracis UDP-GlcNAc 2-epimerase, its substrate UDP-GlcNAc and the reaction intermediate UDP, showed direct interactions between UDP and its substrate, and between the complex and highly conserved enzyme residues, identifying the allosteric site of the enzyme. The binding of UDP-GlcNAc is associated with conformational changes in the active site of the enzyme. Kinetic data and mutagenesis of the highly conserved UDP-GlcNAc-interacting residues confirm their importance in the substrate binding and catalysis of the enzyme. This constitutes the first example to our knowledge, of an enzymatic allosteric activation by direct interaction between the substrate and the allosteric activator.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.