Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P30044 (antioxidant enzyme)
 8,037 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

4-Aminoantipyrine (AAP) is scarcely administered as an analgesic drug because of the potential side effects. The residue of AAP in the environment possesses a potential threat to human health. In this article, the binding mode of AAP with the important antioxidant enzyme catalase (CAT) was investigated using spectroscopic and molecular docking methods. AAP can interact with CAT to form an AAP-CAT complex. The binding constant, number of binding sites and thermodynamic parameters were measured, which indicated that AAP could spontaneously bind with CAT through electrostatic forces with one binding site. Molecular docking results revealed that AAP bound into the CAT central cavity. UV-visible absorption, synchronous fluorescence and circular dichroism (CD) results provide data concerning conformational and some microenvironmental changes of CAT. Furthermore, the binding of AAP can inhibit CAT activity in erythrocytes. The present study provides direct evidence at a molecular level to show that exposure to AAP could induce changes in the enzyme CAT structure and function. The estimated methods in this work can be applied to characterize interactions of enzyme systems and other pollutants and drugs.
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PMID:Molecular interaction between 4-aminoantipyrine and catalase reveals a potentially toxic mechanism of the drug. 2193 40

4-Aminoantipyrine (AAP) is scarcely administered as an analgesic drug because of side effects. The residue of AAP in the environment is potentially harmful. To evaluate the toxicity of AAP from molecular level, the effects of AAP on the important antioxidant enzyme copper-zinc superoxide dismutase (Cu/ZnSOD) were explored using spectroscopic and molecular modeling methods. AAP can spontaneously bind with Cu/ZnSOD with one binding site to form AAP-Cu/ZnSOD complex through hydrogen bond and van der Waals forces. The molecular docking simulation revealed that AAP bound into the Cu/ZnSOD interface of two subdomains, which induced some conformational and microenvironmental changes of Cu/ZnSOD and further caused the inhibition of Cu/ZnSOD activity. The present study provides important insights into toxic mechanism of AAP with Cu/ZnSOD. The estimated research route can be applied to characterize interactions of enzyme systems and other pollutants and drugs.
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PMID:Insights into potentially toxic effects of 4-aminoantipyrine on the antioxidant enzyme copper-zinc superoxide dismutase. 2405 43