Abstract
Background Aldehdyde dehydrogenase-2 (ALDH2) is essential for the detoxification of ethanol in the liver but also catalyzes vascular 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 of efficacy after prolonged treatment, and there is strong evidence that this results from mechanism-based inactivation of ALDH2 by GTN. The precise mechanism of the ALDH2/GTN reaction as well as the identity of the inactivated enzyme species is still elusive.
Highlights
Aldehdyde dehydrogenase-2 (ALDH2) is essential for the detoxification of ethanol in the liver and catalyzes vascular bioactivation of nitroglycerin to its active metabolite nitric oxide (NO), which causes vasodilation through accumulation of cyclic GMP
Vascular bioactivation of nitroglycerin: reaction mechanism revealed by crystal structure of aldehyde dehydrogenase-2
GTN is bound to the active site by hydrogen bonds to the so-called oxyanion hole, to Gln268 to Ser301 and by hydrophobic interactions
Summary
Aldehdyde dehydrogenase-2 (ALDH2) is essential for the detoxification of ethanol in the liver and catalyzes vascular bioactivation of nitroglycerin (glycerol trinitrate, GTN) to its active metabolite nitric oxide (NO), which causes vasodilation through accumulation of cyclic GMP. Vascular bioactivation of nitroglycerin: reaction mechanism revealed by crystal structure of aldehyde dehydrogenase-2 From 18th Scientific Symposium of the Austrian Pharmacological Society (APHAR). Joint meeting with the Croatian, Serbian and Slovenian Pharmacological Societies.
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