NOX3 complex:RAC1:GTP generates superoxide from oxygen

Stable Identifier
Homo sapiens
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While NOX3:CYBA complex has constitutive NADPH oxidase activity, the presence of NCF1, NCF2 or NOXA1 and RAC1:GTP enhances the production of superoxide O2- by the NOX3:CYBA complex. When NCF1 is replaced with NOXO1, RAC1:GTP becomes dispensible for the full activation of the NOX3 complex (Ueno et al. 2005, Ueyama et al. 2006, Miyano and Sumimoto 2007, Kao et al. 2008)

Literature References
PubMed ID Title Journal Year
16507994 Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases

Geiszt, M, Ueyama, T, Leto, TL

Mol. Cell. Biol. 2006
15824103 The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators

Takeya, R, Miyano, K, Kikuchi, H, Sumimoto, H, Ueno, N

J. Biol. Chem. 2005
18347018 Identification of a conserved Rac-binding site on NADPH oxidases supports a direct GTPase regulatory mechanism

Bohl, B, Taylor, RM, Gianni, D, Bokoch, GM, Kao, YY

J. Biol. Chem. 2008
17583407 Role of the small GTPase Rac in p22phox-dependent NADPH oxidases

Miyano, K, Sumimoto, H

Biochimie 2007
Catalyst Activity

superoxide-generating NAD(P)H oxidase activity of NOX3 complex:RAC1:GTP [plasma membrane]

Orthologous Events
Cross References
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