ArticleBiochemistry2015
An ordered water channel in Staphylococcus aureus FabI: unraveling the mechanism of substrate recognition and reduction.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 30 citations in OpenAlex.
- Underexplored Ligand-Binding Features of FabI From Staphylococcus aureus and Escherichia coli: A Comparative Pharmacophoric Modeling and Surface Mapping Approach.ChemMedChem · 2026Article
- Antimicrobial potential and rhodamine B dye degradation using graphitic carbon nitride and polyvinylpyrrolidone doped bismuth tungstate supported with in silico molecular docking studies.Scientific reports · 2023Article
- Efficient Dye Degradation and Antibacterial Activity of Carbon Dots/Chitosan-Doped LaACS omega · 2023Article
- Molecular Modelling Study and Antibacterial Evaluation of Diphenylmethane Derivatives as Potential FabI Inhibitors.Molecules (Basel, Switzerland) · 2023Article
- Article
- Structure and Candidate Biosynthetic Gene Cluster of a Manumycin-Type Metabolite fromJournal of natural products · 2022Review
- Characterization of protein-ligand binding interactions of enoyl-ACP reductase (FabI) by native MS reveals allosteric effects of coenzymes and the inhibitor triclosan.Protein science : a publication of the Protein Society · 2022Article
- Bacterial Enoyl-Reductases: The Ever-Growing List of Fabs, Their Mechanisms and Inhibition.Frontiers in microbiology · 2022Review
- Comparative Study of Selenides and Tellurides of Transition Metals (Nb and Ta) with Respect to its Catalytic, Antimicrobial, and Molecular Docking Performance.Nanoscale research letters · 2020Article
- The genome of a Bacteroidetes inhabitant of the human gut encodes a structurally distinct enoyl-acyl carrier protein reductase (FabI).The Journal of biological chemistry · 2020Article
- Ligand- and Structure-Based Approaches of Escherichia coli FabI Inhibition by Triclosan Derivatives: From Chemical Similarity to Protein Dynamics Influence.ChemMedChem · 2019Article
- Article
- Benzimidazole-Based FabI Inhibitors: A Promising Novel Scaffold for Anti-staphylococcal Drug Development.ACS infectious diseases · 2017Article
- Correlating Drug-Target Kinetics andChemical science · 2016Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
One third of all drugs in clinical use owe their pharmacological activity to the functional inhibition of enzymes, highlighting the importance of enzymatic targets for drug development. Because of the close relationship between inhibition and catalysis, understanding the recognition and turnover of enzymatic substrates is essential for rational drug design. Although the Staphylococcus aureus enoyl-acyl carrier protein reductase (saFabI) involved in bacterial fatty acid biosynthesis constitutes a very promising target for the development of novel, urgently needed anti-staphylococcal agents, the substrate binding mode and catalytic mechanism remained unclear for this enzyme. Using a combined crystallographic, kinetic, and computational approach, we have explored the chemical properties of the saFabI binding cavity, obtaining a consistent mechanistic model for substrate binding and turnover. We identified a water-molecule network linking the active site with a water basin inside the homo-tetrameric protein, which seems to be crucial for the closure of the flexible substrate binding loop as well as for an effective hydride and proton transfer during catalysis. On the basis of our results, we also derive a new model for the FabI-ACP complex that reveals how the ACP-bound acyl-substrate is injected into the FabI binding crevice. These findings support the future development of novel FabI inhibitors that target the FabI-ACP interface leading to the disruption of the interaction between these two proteins.
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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.