Effect of indole-3-acetic acid on the kinetics of horseradish peroxidase catalyzed scopoletin oxidation.
The kinetics of horseradish peroxidase catalyzed of scopoletin oxidation were observed to be sigmoidal. The apparent KmS for scopoletin is 0.9 mM. Inhibition of scopoletin oxidation by indole-3-acetic acid (IAA) appears to be non competitive. Non competitive inhibition by IAA suggests a more significant role of the peroxidase protein matrix in regulating the activity of the heme moiety.
D006735:Horseradish Peroxidase / Q000378:metabolism*; D007210:Indoleacetic Acids / Q000494:pharmacology*; D007700:Kinetics; D010544:Peroxidases / Q000378:metabolism*; D012603:Scopoletin / Q000378:metabolism*; D014468:Umbelliferones / Q000378:metabolism*
D007210:Indoleacetic Acids; D014468:Umbelliferones; D006735:Horseradish Peroxidase; D010544:Peroxidases; D012603:Scopoletin