55.0% inhibition at 0.004 mM, competitively inhibits the enzyme by binding to the active site, have a protective effect against reactive oxygen species in cells, structure-function relationship, computational molecular docking, overview
COMT from liver, using 2-hydroxyestradiol as substrate, in Tris-HCl buffer (10 mM, pH 7.4), at 37Â°C; COMT from liver, using 4-hydroxyestradiol as substrate, in Tris-HCl buffer (10 mM, pH 7.4), at 37Â°C
CAPE, an active component of propolis, 75% inhibition at 0.01 mM, the competitive inhibitor blocks the substrate entrance, preventing substrate from approaching the active site, but CAPE does not have chelate interaction with HpPDF and does not disrupt the metal-dependent catalysis
The activities of liver adenosine deaminase, xanthine oxidase, catalase, superoxide dismutase enzymes and the levels of malondialdehyde and nitric oxide after cisplatin toxicity in rats: protective effect of caffeic acid phenethyl ester
Yilmaz, H.R.; Sogut, S.; Ozyurt, B.; Ozugurlu, F.; Sahin, S.; Isik, B.; Uz, E.; Ozyurt, H.