ReviewFrontiers in molecular biosciences2022
Advances in UDP-N-Acetylglucosamine Enolpyruvyl Transferase (MurA) Covalent Inhibition.
Review in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Metabolism-Based Biomarkers for Rapid Phenotypic Antibiotic Susceptibility Testing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Optimization of Thyme, Cinnamon, and Black Seed Oil Combinations for Enhanced Antibacterial and Antioxidant Efficacy: Mixture Design and In Silico Insights.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Metagenomic Comparison of Bat Colony Resistomes Across Anthropogenic and Pristine Habitats.Antibiotics (Basel, Switzerland) · 2026Article
- Dual Mechanisms of Action of a Halogenated Allyl Fatty Acid against Methicillin-ResistantACS omega · 2025Article
- Role of UDP-N-acetylmuramic acid in the regulation of MurA activity revealed by molecular dynamics simulations.Protein science : a publication of the Protein Society · 2024Article
- Genetic interaction mapping reveals functional relationships between peptidoglycan endopeptidases and carboxypeptidases.PLoS genetics · 2024Article
- Inhibition of MurA Enzyme fromACS omega · 2023Article
- Molecular modelling and site-directed mutagenesis provide insight into saccharide pyruvylation by the Paenibacillus alvei CsaB enzyme.Scientific reports · 2023Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptidoglycan is a cross-linked polymer responsible for maintaining the bacterial cell wall integrity and morphology in Gram-negative and Gram-positive bacteria. The peptidoglycan pathway consists of the enzymatic reactions held in three steps: cytoplasmic, membrane-associated, and periplasmic. The Mur enzymes (MurA-MurF) are involved in a cytoplasmic stage. The UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) enzyme is responsible for transferring the enolpyruvate group from phosphoenolpyruvate (PEP) to UDP-N-acetylglucosamine (UNAG) to form UDP-N-acetylglucosamine enolpyruvate (EP-UNAG). Fosfomycin is a natural product analogous to PEP that acts on the MurA target enzyme via binding covalently to the key cysteine residue in the active site. Similar to fosfomycin, other MurA covalent inhibitors have been described with a warhead in their structure that forms a covalent bond with the molecular target. In MurA, the nucleophilic thiolate of Cys115 is pointed as the main group involved in the warhead binding. Thus, in this minireview, we briefly describe the main recent advances in the design of MurA covalent inhibitors.
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