Abstract
Biochemical and X-ray crystallographic studies confirmed that hydroxyquinoline derivatives identified by virtual screening were actually covalent inhibitors of the MIF tautomerase. Adducts were formed by N-alkylation of the Pro-1 at the catalytic site with a loss of an amino group of the inhibitor.
MeSH terms
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Crystallography, X-Ray
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Drug Discovery*
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Drug Evaluation, Preclinical / methods*
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Hydroxyquinolines / chemical synthesis
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Hydroxyquinolines / chemistry
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Hydroxyquinolines / pharmacology*
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Intramolecular Oxidoreductases / antagonists & inhibitors*
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Macrophage Migration-Inhibitory Factors / antagonists & inhibitors*
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Models, Molecular
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Molecular Structure
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Structure-Activity Relationship
Substances
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Enzyme Inhibitors
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Hydroxyquinolines
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Macrophage Migration-Inhibitory Factors
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Intramolecular Oxidoreductases