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Background Mitochondrial aldehyde dehydrogenase (ALDH2) plays an essential role in nitroglycerin (GTN) bioactivation, resulting in formation of nitric oxide (NO) or a related activator of soluble guanylate cyclase (sGC) and consequently in cGMP-mediated vasorelaxation [1]. ALDH2 denitrates GTN to 1,2-glyceryl dinitrate (1,2-GDN) and nitrite but also catalyzes reduction of GTN to nitric oxide (NO) [2]. To elucidate the mechanism of ALDH2-catalyzed GTN bioactivation in relation to the established ALDH2 activities (dehydrogenase, esterase), we compared the function of the wildtype (WT) enzyme with a mutant lacking the general base Glu268 (E268Q).

Role of the general base Glu268 in nitroglycerin bioactivation and mechanism-based superoxide formation by aldehyde dehydrogenase-2