Current Enzyme Inhibition - Volume 11, Issue 2, 2015

Benzenesulfonamide is versatile motif employed for the discovery in the field of medicinal and pharmaceutical chemistry. Over the years of active research, sulfonamide has evolved as important privileged pharmacophore in medicinal chemistry, encompassing a diverse range of biological activities including antiviral, carbonic anhydrase inhibitors, diuretic, and a protease inhibitor, hypoglycemic, anticancer and anti-inflamm Read More

Context: Xanthine oxidase is a key enzyme in purine metabolism with an important role in various pathological conditions including gout and oxidative stress. Many of the synthetic candidates showed remarkable activity with a greater amount of side effects. Thus the search of promising structural core like flavonoids emerged greater attention for the inhibition of xanthine oxidase. Objective: The objective of this review is Read More

P38 kinase has been known to be one of the important and validated targets for inflammatory diseases including rheumatoid arthritis for its vital role in production and release of proinflammatory cytokines including tumor necrosis factor alpha (TNF-α) and interleukin-beta (IL-1β). Pyridinyl group of our reported compounds was replaced by simple phenyl groups and compounds were synthesized and characterized. A dose o Read More

D-Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes the reversible oxidation of D-glyceraldehyde-3-phosphate (G3P) to 1,3-bis-phospho-D-glycerate, and as such participates in the glycolytic conversion of glucose to pyruvic acid in most living organisms. The glycolytic pathway plays an important role in tumor cells, but it is not clear whether the enzyme kinetics of GAPDH or their response to inhibitors, s Read More

Histone Deacetylases (HDACs) are a class of enzymes that has become one of the potential, promising and well established targets for the treatment of cancer. In the present work, a series of pyrimidine hydroxamates were designed and synthesized as novel HDAC inhibitors. The compounds possess diaryl pyrimidine as cap, piperazine as linker and hydroxamate at Zn2+ binding group. These were designed with a Read More

Using wheat germ acid phosphatase and sodium orthovanadate as a competitive inhibitor, a novel method for analyzing reversible inhibition was carried out. Our alternative approach involves plotting the initial velocity at which product is formed as a function of the ratio of substrate concentration to inhibitor concentration at a constant enzyme concentration and constant assay conditions. The concept of initial conce Read More

The paper reports the inhibition kinetics of pig liver carboxylesterase (CE) by two food azo dyes, tartrazine (E 102) and green dye (E102-E132), using ethyl butyrate as substrate. Optimum pH and temperature for pig liver CE were found to be 8.0 and 45°C. The kinetics of CE-catalyzed hydrolysis of ethyl butyrate followed the Haldane model with an optimum substrate concentration of 30 mM. Km and Vmax values were Read More