[HTML][HTML] Phosphorylation of threonine 497 in endothelial nitric-oxide synthase coordinates the coupling of L-arginine metabolism to efficient nitric oxide production
MI Lin, D Fulton, R Babbitt, I Fleming, R Busse… - Journal of biological …, 2003 - ASBMB
There is evidence that endothelial nitric-oxide synthase (eNOS) is regulated by reciprocal
dephosphorylation of Thr 497 and phosphorylation of Ser 1179. To examine the
interrelationship between these sites, cells were transfected with wild-type (WT), T497A,
T497D, S1179D, and T497A/S1179D eNOS and activity, NO release and eNOS localization
were assessed. Although eNOS T497A, S1179D and T497A/S1179D eNOS had greater
enzymatic activity than did WT eNOS in lysates, basal production of NO from cells was …
dephosphorylation of Thr 497 and phosphorylation of Ser 1179. To examine the
interrelationship between these sites, cells were transfected with wild-type (WT), T497A,
T497D, S1179D, and T497A/S1179D eNOS and activity, NO release and eNOS localization
were assessed. Although eNOS T497A, S1179D and T497A/S1179D eNOS had greater
enzymatic activity than did WT eNOS in lysates, basal production of NO from cells was …