Hyoung-Woo Bai

TL;DR: In this article, the authors have cloned and expressed human soluble and membrane-bound COMTs in Escherichia coli and have studied their biochemical characteristics for the O-methylation of a wide array of catechol-containing substrates using s-adenosyl-l-methionine as the methyl donor.

TL;DR: Computational molecular modeling analysis showed that chlorogenic acid and caffeic acid can bind to human soluble COMT at the active site in a similar manner as the catechol estrogen substrates, which means that coffee polyphenols have higher binding affinity for the enzyme than the natural substrates.

TL;DR: It is found that some of the bioflavonoids likely will serve as the naturally occurring cofactors for the COX enzymes in humans, and are the most powerful direct stimulators of the catalytic activity of COX I and II known to date.

TL;DR: Investigation of the effect of two representative dietary compounds, quercetin and myricetin, on plasma and tissue levels of several PG products in normal Sprague-Dawley rats found that these two dietary bioflavonoids could strongly stimulate the formation ofPG products in vivo in a time-dependent manner, and the stimulatory effect was dose-dependent with a unique biphasic pattern.

TL;DR: These findings provide the structural basis for bioflavonoids to function as high-affinity reducing co-substrates of COXs through binding to the peroxidase active site, facilitating electron transfer and enzyme re-activation.