EC Number   |
General Information |
Reference |
|---|
    2.7.1.56 | metabolism |
the enzyme is involved in fructose catabolism |
-, 722543 |
| 2.7.1.56 | physiological function |
both phosphofructokinase-1 subunits Pfk1 and Pfk2 coimmunoprecipitate with vacuolar ATPase in wild-type cells. Upon deletion of one subunit, the other subunit retains binding to V-ATPase. Mutants lacking Pfk1 or Pfk2 grow on glucose and assemble wild-type levels of V-ATPase pumps at the membrane. The pfk2 mutant cells exhibit a partial vacuolar membrane ATPase-deficinet growth phenotype. In vitro ATP-hydrolysis and proton transport are reduced by 35% in Pfk2 mutant membrane fractions, they are normal in pfk1 mutants. In vivo, the Pfk1 and Pfk2 mutant vacuoles are alkalinized and the cytosol acidified. The pH alterations are more dramatic in Pfk2 than Pfk1 mutants at steady state and after readdition of glucose to glucose-deprived cells. Glucose-dependent reassembly is 50% reduced in Pfk2 mutants, and the vacuolar lumen is not acidified after reassembly. Regulator of ATPase of vaculoe and endosome RAVE-assisted glucose-dependent reassembly and/or glucose signals are disturbed in Pfk2 mutants |
-, 738617 |
| 2.7.1.56 | physiological function |
nucleoredoxin, a thioredoxin-related oxidoreductase, is a interacting partner of PFK1. NRX binds directly to PFK1, and endogenous NRX and PFK1 interact in vivo. In NRX-/- mouse embryonic fibroblasts, the oligomerization status of PFK1 is altered and the catalytic activity of PFK1 is decreased. NRX deficiency augments levels of NADPH and reduced glutathione. NRX -/- mouse embryonic fibroblasts are significantly more resistant to oxidative stress than NRX+/+ mouse embryonic fibroblasts |
737595 |
