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An alternative view is that the oxidase elevates the pH in the vacuole to about 9.0, which is optimal for the neutral proteases that degranulate from the cytoplasmic granules (where they are inactive at pH ~5.5) and it pumps potassium into the vacuole, which solubilises the enzymes, and it is the activated proteases that kill and digest the ...
n/a Ensembl ENSG00000255346 n/a UniProt Q96PH1 n/a RefSeq (mRNA) NM_001184779 NM_001184780 NM_024505 n/a RefSeq (protein) NP_001171708 NP_001171709 NP_078781 n/a Location (UCSC) Chr 15: 68.93 – 69.06 Mb n/a PubMed search n/a Wikidata View/Edit Human NADPH oxidase, EF-hand calcium binding domain 5, also known as NOX5, is a protein which in humans is encoded by the NOX5 gene. Function NOX5 is ...
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP [1] [2] or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form, whereas NADP + is the ...
NAD + may also be added onto cellular RNA as a 5'-terminal modification. [72] The structure of cyclic ADP-ribose. Another function of this coenzyme in cell signaling is as a precursor of cyclic ADP-ribose, which is produced from NAD + by ADP-ribosyl cyclases, as part of a second messenger system. [73]
The ratio of NADPH:NADP + is the primary mode of regulation for the enzyme and is normally about 100:1 in liver cytosol [citation needed]. This makes the cytosol a highly-reducing environment. An NADPH-utilizing pathway forms NADP +, which stimulates Glucose-6-phosphate dehydrogenase to produce more NADPH.
p22phox Protein, also known as the human neutrophil cytochrome b light chain (CYBA), is an essential component of the membrane-associated enzyme phagocyte NADPH-oxidase [1] This enzyme uses NADH or NADPH as the electron donor for the one electron reduction of oxygen to produce superoxide anion, a reactive oxygen species (ROS), [2] and a functionally important step for the antimicrobial ...
Cytochrome P450 reductase (also known as NADPH:ferrihemoprotein oxidoreductase, NADPH:hemoprotein oxidoreductase, NADPH:P450 oxidoreductase, P450 reductase, POR, CPR, CYPOR) is a membrane-bound enzyme required for electron transfer from NADPH to cytochrome P450 [5] and other heme proteins including heme oxygenase in the endoplasmic reticulum [6] of the eukaryotic cell.
NADH:ubiquinone reductase (non-electrogenic) (EC 1.6.5.9, NDH-2, ubiquinone reductase, coenzyme Q reductase, dihydronicotinamide adenine dinucleotide-coenzyme Q reductase, DPNH-coenzyme Q reductase, DPNH-ubiquinone reductase, NADH-coenzyme Q oxidoreductase, NADH-coenzyme Q reductase, NADH-CoQ oxidoreductase, NADH-CoQ reductase) is an enzyme with systematic name NADH:ubiquinone oxidoreductase.