ArticleMolecules (Basel, Switzerland)2014
Inhibition and biochemical characterization of methicillin-resistant Staphylococcus aureus shikimate dehydrogenase: an in silico and kinetic study.
Article in Molecules (Basel, Switzerland), 2014. 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.
- Determination of Potential Inhibitors againstCurrent pharmaceutical design · 2026Review
- A Scorecard for Information Synthesis in Multiple Experimental Conditions: Application to Bacterial Biofilm Matrix Transcriptomics.Current microbiology · 2025Article
- Characterization of Natural Products as Inhibitors of Shikimate Dehydrogenase from Methicillin-ResistantBiomolecules · 2025Article
- Identification of potential inhibitors againstJournal of enzyme inhibition and medicinal chemistry · 2024Article
- Deletion Mutants ofPathogens (Basel, Switzerland) · 2021Article
- Characterization of Schu S4Virulence · 2020Article
- Review
- Synthesis, biological activity and molecular modelling studies of shikimic acid derivatives as inhibitors of the shikimate dehydrogenase enzyme of Escherichia coli.Journal of enzyme inhibition and medicinal chemistry · 2018Article
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Authors and funding
7 authors.
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Abstract
Methicillin-resistant Staphylococcus auerus (MRSA) strains are having a major impact worldwide, and due to their resistance to all β-lactams, an urgent need for new drugs is emerging. In this regard, the shikimate pathway is considered to be one of the metabolic features of bacteria and is absent in humans. Therefore enzymes involved in this route, such as shikimate dehydrogenase (SDH), are considered excellent targets for discovery of novel antibacterial drugs. In this study, the SDH from MRSA (SaSDH) was characterized. The results showed that the enzyme is a monomer with a molecular weight of 29 kDa, an optimum temperature of 65 °C, and a maximal pH range of 9-11 for its activity. Kinetic studies revealed that SDH showed Michaelis-Menten kinetics toward both substrates (shikimate and NADP+). Initial velocity analysis suggested that SaSDH catalysis followed a sequential random mechanism. Additionally, a tridimensional model of SaSDH was obtained by homology modeling and validated. Through virtual screening three inhibitors of SaSDH were found (compounds 238, 766 and 894) and their inhibition constants and mechanism were obtained. Flexible docking studies revealed that these molecules make interactions with catalytic residues. The data of this study could serve as starting point in the search of new chemotherapeutic agents against MRSA.
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