[HTML][HTML] Enhanced electron flux and reduced calmodulin dissociation may explain “calcium-independent” eNOS activation by phosphorylation
TJ McCabe, D Fulton, LJ Roman, WC Sessa - Journal of Biological …, 2000 - ASBMB
Bovine endothelial nitric oxide synthase (eNOS) is phosphorylated directly by the protein
kinase Akt at serine 1179. Mutation of this residue to the negatively charged aspartate
(S1179D eNOS) increases nitric oxide (NO) production constitutively, in the absence of
agonist challenge. Here, we examine the potential mechanism of how aspartate at 1179
increases eNOS activity using purified proteins. Examination of NO production and
cytochrome creduction resulted in no substantial changes in theK m/EC 50 for l-arginine …
kinase Akt at serine 1179. Mutation of this residue to the negatively charged aspartate
(S1179D eNOS) increases nitric oxide (NO) production constitutively, in the absence of
agonist challenge. Here, we examine the potential mechanism of how aspartate at 1179
increases eNOS activity using purified proteins. Examination of NO production and
cytochrome creduction resulted in no substantial changes in theK m/EC 50 for l-arginine …