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Literature summary for 1.6.3.1 extracted from

  • Bissonnette, S.A.; Glazier, C.M.; Stewart, M.Q.; Brown, G.E.; Ellson, C.D.; Yaffe, M.B.
    Phosphatidylinositol 3-phosphate-dependent and -independent functions of p40phox in activation of the neutrophil NADPH oxidase (2008), J. Biol. Chem., 283, 2108-2119.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
phosphatidylinositol 3-phosphate subunit p40phox phosphatidylinositol 3-phosphate binding PX domain has phosphatidylinositol 3-phosphate-dependent and -independent functions. Translocation of subunit p67phox requires the PX domain but not 3-phosphoinositide binding. Activation of the oxidase by p40phox, however, requires both phosphatidylinositol 3-phosphate binding and an Src homology 3 domain competent to bind to poly-Pro ligands Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information depletion of endogenous subunit p40phoxusing lentiviral short hairpin RNA reduces reactive oxygen species production and impairs bacterial killing by phagolysosomes under conditions where subunit p67phox levels remain constant. Depletion of p40phox reduces both the maximal rate and total amount of ROS produced without altering theKM value of the oxidase forNADPH Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.015
-
NADPH subunit p40phox-depleted cytosol in the absencee of recombinant wild-type p40phox, pH 7.3, 37°C Homo sapiens
0.024
-
NADPH subunit p40phox-depleted cytosol in the presence of recombinant wild-type p40phox, pH 7.3, 37°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
PLB-985 cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADPH + H+ + O2
-
Homo sapiens NADP+ + H2O2
-
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