ArticleThe Journal of biological chemistry2014
Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from Escherichia coli.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Analysis of the regulation of undecaprenyl diphosphate dephosphorylation in Escherichia coli.FEBS open bio · 2025Article
- Real-Time Biosynthetic Reaction Monitoring Informs the Mechanism of Action of Antibiotics.Journal of the American Chemical Society · 2024Article
- Structure, catalysis, and inhibition mechanism of prenyltransferase.IUBMB life · 2021Review
- Virulence of the emerging pathogen,Future microbiology · 2020Article
- Identification of a Phenylthiazole Small Molecule with Dual Antifungal and Antibiofilm Activity Against Candida albicans and Candida auris.Scientific reports · 2019Article
- Minimal exposure of lipid II cycle intermediates triggers cell wall antibiotic resistance.Nature communications · 2019Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling.Nature communications · 2018Article
- Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis.Nature communications · 2018Article
- Phenylthiazole Antibacterial Agents Targeting Cell Wall Synthesis Exhibit Potent Activity in Vitro and in Vivo against Vancomycin-Resistant Enterococci.Journal of medicinal chemistry · 2017Article
- Bacteriological profiling of diphenylureas as a novel class of antibiotics against methicillin-resistant Staphylococcus aureus.PloS one · 2017Article
- Depletion of Undecaprenyl Pyrophosphate Phosphatases Disrupts Cell Envelope Biogenesis in Bacillus subtilis.Journal of bacteriology · 2016Article
- Bacterial Cell Growth Inhibitors Targeting Undecaprenyl Diphosphate Synthase and Undecaprenyl Diphosphate Phosphatase.ChemMedChem · 2016Article
- Isoprenoid Biosynthesis Inhibitors Targeting Bacterial Cell Growth.ChemMedChem · 2016Article
- The Membrane Steps of Bacterial Cell Wall Synthesis as Antibiotic Targets.Antibiotics (Basel, Switzerland) · 2016Review
- New Insight into the Catalytic Mechanism of Bacterial MraY from Enzyme Kinetics and Docking Studies.The Journal of biological chemistry · 2016Article
- Article
- Core Steps of Membrane-Bound Peptidoglycan Biosynthesis: Recent Advances, Insight and Opportunities.Antibiotics (Basel, Switzerland) · 2015Review
- Determining the N-terminal orientations of recombinant transmembrane proteins in the Escherichia coli plasma membrane.Scientific reports · 2015Article
- Large-scale determination of previously unsolved protein structures using evolutionary information.eLife · 2015Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Undecaprenyl pyrophosphate phosphatase (UppP), an integral membrane protein, catalyzes the dephosphorylation of undecaprenyl pyrophosphate to undecaprenyl phosphate, which is an essential carrier lipid in the bacterial cell wall synthesis. Sequence alignment reveals two consensus regions, containing glutamate-rich (E/Q)XXXE plus PGXSRSXXT motifs and a histidine residue, specific to the bacterial UppP enzymes. The predicted topological model suggests that both of these regions are localized near the aqueous interface of UppP and face the periplasm, implicating that its enzymatic function is on the outer side of the plasma membrane. The mutagenesis analysis demonstrates that most of the mutations (E17A/E21A, H30A, S173A, R174A, and T178A) within the consensus regions are completely inactive, indicating that the catalytic site of UppP is constituted by these two regions. Enzymatic analysis also shows an absolute requirement of magnesium or calcium ions in enzyme activity. The three-dimensional structural model and molecular dynamics simulation studies have shown a plausible structure of the catalytic site of UppP and thus provides insights into the molecular basis of the enzyme-substrate interaction in membrane bilayers.
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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.