Mammalian 15-lipoxygenases (ALOX15) are lipid peroxidizing enzymes that exhibit variable functionality in different cancer and inflammation models. The pathophysiological role of linoleic acid- arachidonic acid-derived ALOX15 metabolites rendered this enzyme a target for pharmacological research. Several indole imidazole derivatives inhibit the catalytic activity rabbit substrate-specific manne...

conclusions all plants could inhibit mushroom tyrosinase, but more investigations on human tyrosinase and clinical studies are needed. results the hydroalcoholic extract of p. alkekengi showed the most tyrosinase inhibitory effect with ic50 of 0.09 mg/ml vs. 0.38, 0.38 and 2.82 mg/ml of b. persicum, a. rosea and m. vulgare, respectively. m. vulgare exhibited uncompetitive inhibition and other p...

b-biotype bemisia tabaci is a severe insect pest worldwide in many ornamental, agricultural, and horticultural crops. control of this insect is obstructed by resistance to many acetylcholinesterase (ache)-inhibiting insecticides, such as organophosphates and carbamates. in the present work, we evaluated the acetylcholinesterase inhibitory activity of six monoterpenoids namely α-pinene, terpineo...

The mechanism of reaction of human erythrocyte hypoxanthine-guanine phosphoribosyltransferase was investigated by initial velocity, product inhibition, and isotope exchange studies. Although initial velocity data are compatible with a mechanism involving binary enzyme-substrate complexes, the product inhibition and isotope exchange studies indicate that the reaction is ordered with the formatio...

mercury is one of the three major environmental metal poisons, and mercuric chloride is a highly reactive compound which can harm cells by a variety of mechanisms including direct interaction with sulphydryl groups of proteins and enzymes, therefore affecting the enzymatic activity. this study focused on the effect of hg++ on horseradish peroxidase (donor: hydrogen peroxide oxidoreductase, ec 1...

Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase undergoes significant inhibition of activity with increasing concentrations of its substrate, hydroxypyruvic acid phosphate. The enzyme also displays an unusual dual pH optimum. A significant decrease in the K(i) for substrate inhibition at pH values corresponding to the valley between these optima is responsible for this phenomena. ...