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. 2013 Jul 25;9:401–428. doi: 10.2147/VHRM.S33053

Figure 2.

Figure 2

Subunit composition of the NADPH oxidase isoforms. The catalytic core subunits of the complex (NOX1–5 and DUOX1–2) are shown in grey and their stabilization partners (p22phox and DUOX activator 1 and 2) are shown in magenta. NOX4 is the only isoform that produces hydrogen peroxide instead of superoxide anion. The regulatory cytosolic subunits of each isoform are shown in each case: p40phox, p47phox, p67phox, NOX organizer 1 (NOXO1), NOX activator 1 (NOXA1), small GTPase (Rac), polymerase delta-interacting protein 2 (POLDIP2), a p47phox analog tyrosine kinase substrate with 4/5 SH3 domains (TKS4/5), EF hand motifs, (calcium-binding motifs composed of two helixes (E and F) joined by a loop), calmodulin (CaM) and heat shock protein 90 (HSP90). On DUXO1 and DUOX2 a putative additional amino-terminal transmembrane domain and extracellular peroxidase-like region (PLD) are shown.

Abbreviations: C-ter, carboxy-terminal; FAD, flavin adenine dinucleotide; GTPase, guanine triphosphate hydrolase; NADPH, nicotinamide adenine dinucleotide phosphate; N-ter, amino-terminal; O2, oxygen; H2O2, hydrogen peroxide; O2−, superoxide; SH3, Src-homology region 3.