EC Number |
General Information |
Reference |
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1.6.5.2 | evolution |
enzyme FerB is listed in the NADPH-dependent FMN reductase family, PF03358 |
-, 743659 |
1.6.5.2 | metabolism |
NAD(P)H quinone oxidoreductase 1-mediated targeting of homocysteine-induced endoplasmic reticulum protein Herp to the proteasome is involved in Herp degradation. NQO1 is a target of nuclear factor E2-related factor Nrf2, which regulates cellular reactive oxygen speciesNrf2 |
744232 |
1.6.5.2 | more |
importance of residue Ser11, Arg13, Ser16 and Asn18 for FMN binding, and of the tyrosine residues Tyr46 and Tyr78 and possibly also Ser113 for capturing the isoalloxazine ring of FMN. FMN and NADH docking, overview |
-, 743659 |
1.6.5.2 | more |
the homodimeric flavoprotein is unique among reductases, as it catalyzes the direct two-electron reduction of a wide variety quinones using NADH or NADPH as cofactor. Substrate docking studies, overview |
724356 |
1.6.5.2 | physiological function |
a gene disruption strain is unable to grow with ethanol-sulfate. The FlxABCD-HdrABC (heterodisulfide reductase) proteins are essential for NADH oxidation during growth on ethanol, while in fermentation they operate in reverse, reducing NAD+ for ethanol production |
-, 742382 |
1.6.5.2 | physiological function |
artificial overexpression of NQO1 is able to increase the level of hydroquinone and cell sensitivity to IPI-504. NQO1 activity is not a determinant of IPI-504 activity |
713005 |
1.6.5.2 | physiological function |
double knockout plants of both NQR and b-type cytochrome AIR12 generate more O2- radicals and germinate faster than the single mutant affected in AIR12. NQR and AIR12 may interact via the quinone, allowing an electron transfer from cytosolic NAD(P)H to apoplastic monodehydroascorbate |
746160 |
1.6.5.2 | physiological function |
FerB from Paracoccus denitrificans is a soluble cytoplasmic flavoprotein that accepts redox equivalents from NADH or NADPH and transfers them to various acceptors such as quinones, ferric complexes and chromate |
-, 743659 |
1.6.5.2 | physiological function |
in addition to protection of b-cells from toxic concentrations of the redox cycling quinone menadione, NQO1 also regulates the basal level of reduced-to-oxidized nucleotides |
746535 |
1.6.5.2 | physiological function |
isoform NDA2 drives cyclic electron flow, chlororespiration, and the generation of an H+ gradient across the thylakoid membranes. N deprivation elicits a doubling of the rate of NDA2-dependent cyclic electron flow, with little contribution from PGR5/PGRL1-dependent cyclic electron flow. Stimulation of NDA2-dependent chlororespiration affords additional relief from the elevated reduction state associated with N deprivation through plastid terminal oxidase-dependent water synthesis |
743497 |