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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.

SUBMITTER: Heiss EH

PROVIDER: S-EPMC4401012 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Regulation of eNOS enzyme activity by posttranslational modification.

Heiss Elke H EH Dirsch Verena M VM

Current pharmaceutical design 20140101 22

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, cooper ...[more]

PMID: 24180389

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