Learn More
Aldehyde dehydrogenase-2 (ALDH2) catalyzes the bioactivation of nitroglycerin (glyceryl trinitrate, GTN) in blood vessels, resulting in vasodilation by nitric oxide (NO) or a related species. Because the mechanism of this reaction is still unclear we determined the three-dimensional structures of wild-type (WT) ALDH2 and of a triple mutant of the protein(More)
Mitochondrial aldehyde dehydrogenase-2 (ALDH2) plays an essential role in nitroglycerin (GTN) bioactivation, resulting in formation of NO or a related activator of soluble guanylate cyclase. ALDH2 denitrates GTN to 1,2-glyceryl dinitrate and nitrite but also catalyzes reduction of GTN to NO. To elucidate the relationship between ALDH2-catalyzed GTN(More)
Background Aldehdyde dehydrogenase-2 (ALDH2) is essential for the detoxification of ethanol in the liver but also catalyzes vas-cular bioactivation of nitroglycerin (glycerol trinitrate, GTN) to its active metabolite nitric oxide (NO), which causes vasodilation through accumulation of cyclic GMP. The clinical use of GTN as a vasodilator is hampered by loss(More)
Background The East Asian variant of mitochondrial aldehyde dehy-drogenase (ALDH2) exhibits significantly reduced dehy-drogenase, esterase and nitroglycerin (GTN) reductase activities [1]. The small molecule Alda-1 was reported to partly restore low acetaldehyde dehydrogenase activity of this variant [2]. In the present study we compared the wild-type(More)
  • 1