The regulation of endothelial NO synthase (eNOS) employs multiple different cellular control mechanisms impinging on level
and activity of the enzyme. This review aims at summarizing the current knowledge on the posttranslational modifications of eNOS, including
acylation, nitrosylation, phosphorylation, acetylation, glycosylation and glutathionylation. Sites, mediators and impact on enzyme
localization and activity of the single modifications will be discussed. Moreover, interdependence, cooperativity and competition between
the different posttranslational modifications will be elaborated with special emphasis on the susceptibility of eNOS to metabolic cues.