Uncoupled eNOS favours the formation of superoxide

Stable Identifier
R-HSA-1497810
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
BH2 may compete with BH4 to bind eNOS, uncoupling eNOS leading to the formation of superoxide rather than nitric oxide. BH2, the oxidised form of BH4, cannot contribute electrons to heme in the reductase domain of eNOS, thereby uncoupling it from arginine oxidation and producing superoxide from oxygen instead (Vasquez-Vivar et al. 2002).
Literature References
PubMed ID Title Journal Year
11879202 The ratio between tetrahydrobiopterin and oxidized tetrahydrobiopterin analogues controls superoxide release from endothelial nitric oxide synthase: an EPR spin trapping study

Kalyanaraman, B, Joseph, J, Whitsett, J, Vásquez-Vivar, J, Martasek, P

Biochem J 2002
Participants
Participates
Catalyst Activity

superoxide-generating NAD(P)H oxidase activity of p-S1177-eNOS:CaM:HSP90:p-AKT1:BH2 [plasma membrane]

Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
Cite Us!