title: Regulation of eNOS enzyme activity by posttranslational modification.
abstract: 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.
authors.forename: Elke H
authors.initials: EH
authors.lastname: Heiss
authors.affiliation: University of Vienna, Department of Pharmacognosy, Althanstrasse14, 1090 Vienna, Austria. elke.heiss@univie.ac.at.
authors.forename: Verena M
authors.initials: VM
authors.lastname: Dirsch
mesh_terms: D006801:Humans; D052250:Nitric Oxide Synthase Type III / Q000737:chemistry* / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
chemical_list: D052250:Nitric Oxide Synthase Type III