ArticleThe protein journal2024
Structural and Biochemical Studies on Klebsiella Pneumoniae Enoyl-ACP Reductase (FabI) Suggest Flexible Substrate Binding Site.
Article in The protein journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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Who cites it
4 citing papers in PubMed, 2 citations in OpenAlex.
- Novel salivary biomarkers of Alzheimer's disease identified by integrated metabolomics and microbiomics analysis.Clinical oral investigations · 2026Article
- Structural and Biochemical Characterization ofACS bio & med chem Au · 2026Article
- Cloning, Expression, Purification and Biological Activity Analysis of Recombinant Helicobacter pylori FabI as a Drug Target.Molecular biotechnology · 2026Article
- Molecular docking analysis of FAS II fromBioinformation · 2026Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Klebsiella pneumoniae, a bacterial pathogen infamous for antibiotic resistance, is included in the priority list of pathogens by various public health organizations due to its extraordinary ability to develop multidrug resistance. Bacterial fatty acid biosynthesis pathway-II (FAS-II) has been considered a therapeutic drug target for antibacterial drug discovery. Inhibition of FAS-II enzyme, enoyl-acyl carrier protein reductase, FabI, not only inhibits bacterial infections but also reverses antibiotic resistance. Here, we characterized Klebsiella pneumoniae FabI (KpFabI) using complementary experimental approaches including, biochemical, x-ray crystallography, and molecular dynamics simulation studies. Biophysical studies shows that KpFabI organizes as a tetramer molecular assembly in solution as well as in the crystal structure. Enzyme kinetics studies reveal a distinct catalytic property towards crotonyl CoA and reducing cofactor NADH. Michaelis-Menten constant (K
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Registered trials
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