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Literature summary extracted from

  • Lin, H.C.; Tsai, S.H.; Chen, C.S.; Chang, Y.C.; Lee, C.M.; Lai, Z.Y.; Lin, C.M.
    Structure-activity relationship of coumarin derivatives on xanthine oxidase-inhibiting and free radical-scavenging activities (2008), Biochem. Pharmacol., 75, 1416-1425.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.3.2 4-Hydroxycoumarin competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview Mus musculus
1.17.3.2 4-methylesculetin competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview Mus musculus
1.17.3.2 7-hydroxy-4-methylcoumarin low competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview Mus musculus
1.17.3.2 7-hydroxycoumarin low competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview Mus musculus
1.17.3.2 allopurinol strong competitive inhibition Mus musculus
1.17.3.2 esculetin strong, competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview Mus musculus
1.17.3.2 additional information coumarin and dihydrocoumarin are poor inhibitors, measurement of combined reactive oxygen species-scavenging and xanthine oxidase-inhibition activities, 3D modeling of the docking of coumarin derivatives on xanthine oxidase, overview Mus musculus
1.17.3.2 scopoletin low competitive inhibition and interaction with the molybdopterin region of the enzyme, structure-function relationship of coumarin derivatives in inhibition of the enzyme, structure-based computer-aided molecular modeling, overview Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.3.2 xanthine + H2O + O2 Mus musculus production of superoxide radicals urate + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.3.2 Mus musculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.3.2 Neuro-2a cell
-
 Mus musculus
-
1.17.3.2 neuroblastoma cell
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.3.2 xanthine + H2O + O2 production of superoxide radicals Mus musculus urate + H2O2
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.17.3.2 37
-
 assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.17.3.2 7
-
 assay at Mus musculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.17.3.2 additional information
-
 additional information inhibition kinetics Mus musculus

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.17.3.2 0.0011
-
 pH 7.0, 37°C, versus xanthine Mus musculus allopurinol
1.17.3.2 0.0781
-
 pH 7.0, 37°C, versus xanthine Mus musculus 4-Hydroxycoumarin