Title : Enhanced electron flux and reduced calmodulin dissociation may explain "calcium-independent" eNOS activation by phosphorylation.

Pub. Date : 2000 Mar 3

PMID : 10692402






4 Functional Relationships(s)
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Protein Name
Organism
1 Bovine endothelial nitric oxide synthase (eNOS) is phosphorylated directly by the protein kinase Akt at serine 1179. Serine nitric oxide synthase 3 Bos taurus
2 Bovine endothelial nitric oxide synthase (eNOS) is phosphorylated directly by the protein kinase Akt at serine 1179. Serine nitric oxide synthase 3 Bos taurus
3 These results suggest that a negative charge imposed at serine 1179, either by phosphorylation or by replacement with aspartate, increases eNOS catalytic activity by increasing electron flux at the reductase domain and by reducing calmodulin dissociation from activated eNOS when calcium levels are low. Serine nitric oxide synthase 3 Bos taurus
4 These results suggest that a negative charge imposed at serine 1179, either by phosphorylation or by replacement with aspartate, increases eNOS catalytic activity by increasing electron flux at the reductase domain and by reducing calmodulin dissociation from activated eNOS when calcium levels are low. Serine nitric oxide synthase 3 Bos taurus