NOX4, NOX5 reduce O2 to O2.-

Stable Identifier
R-HSA-6807557
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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NADPH oxidases 4 and 5 (NOX4, 5) are ER membrane-bound proteins that generates superoxide (O2.-) in endothelial cells (BelAiba et al. 2007). NOX4 functions in association with cytochrome b heterodimer (CYBA:CYBB) on the ER (and nuclear) membrane (Martyn et al. 2006).
Literature References
PubMed ID Title Journal Year
15927447 Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases

von Loehneysen, K, Frederick, LM, Martyn, KD, Dinauer, MC, Knaus, UG

Cell. Signal. 2006
17275676 NOX5 variants are functionally active in endothelial cells

Bickel, C, Pogrebniak, A, Görlach, A, Bonello, S, Banfi, B, Djordjevic, T, Petry, A, Diemer, K, Hess, J, BelAiba, RS

Free Radic. Biol. Med. 2007
Participants
Participates
Catalyst Activity

superoxide-generating NAD(P)H oxidase activity of NOX4, NOX5 [endoplasmic reticulum membrane]

Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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