NADPH oxidase (nicotinamide adenine dinucleotide phosphate oxidase) is a membrane-bound enzyme complex that faces the extracellular space. It can be found in the plasma membrane as well as in the membranes of phagosomes used by neutrophil white blood cells to engulf microorganisms. Human isoforms of the catalytic component of the complex include NOX1, NOX2, NOX3, NOX4, NOX5, DUOX1, and DUOX2.
In enzymology, a NADH peroxidase (EC 22.214.171.124) is an enzyme that catalyzes the chemical reaction. NADH + H + + H 2 O 2 ⇌ NAD + + 2 H 2 O. The presumed function of NADH peroxidase is to inactivate H 2 O 2 generated within the cell, for example by glycerol-3-phosphate oxidase during glycerol metabolism or dismutation of superoxide, before the H 2 O 2 causes damage to essential cellular components.
NADH Oxidase Activity of Indoleamine 2,3-Dioxygenase
The heme enzyme indoleamine 2,3-dioxygenase (IDO) was found to oxidize NADH under aerobic conditions in the absence of other enzymes or reactants. This reaction led to the formation of the dioxygen adduct of IDO and supported the oxidation of Trp to N-formylkynurenine. ...
Enzymatic Assay of NADH OXIDASE FINAL ASSAY CONCENTRATIONS: In a 3.00 ml reaction mix, the final assay concentrations are 51 mM potassium phosphate, 0.07 mM ß-nicotinamide adenine dinucleotide, reduced form, 0.1 mM flavin adenine dinucleotide, 0.003% (w/v) bovine serum albumin, and 0.02 unit NADH oxidase. REFERENCE:
NADPH Oxidase - an overview | ScienceDirect Topics
NADPH oxidase activity is a relatively nonspecific activity displayed by several electron transfer enzymes and dehydrogenases as well. Because many of these enzymes are flavoproteins, a blocking effect of diphenylene iodonium is not discriminative of the NADPH oxidase complex (Laurindo et al., 2002).
A Hemin/G‐Quadruplex Acts as an NADH Oxidase and NADH ...
Enzyme impressionist: A DNAzyme consisting of hemin combined with a G‐quadruplex was shown to mimic the activity of NADH oxidase under aerobic conditions and of NADH peroxidase under anaerobic conditions.Along with these new biocatalytic activities, the hemin/G‐quadruplex complex is also capable of regenerating the biologically important NAD + cofactor in both cycles (see picture).
NADH Oxidase from Bacillus licheniformis lyophilized ...
NADH Oxidase is a surface enzyme with increased oxidative activity in polymorphonuclear leukocytes during phagocytosis. Application NADH Oxidase from Bacillus licheniformis has been used in a study to assess nitrogen assimilation by Bacillus licheniformis growing in chemostat cultures.
NADH oxidase catalyzes the four-electron reduction of molecular oxygen to water by using reducing equivalents from NADH (Eq. 4). By regenerating NAD + for glycolysis, NADH oxidase plays an important metabolic role in the heme-deficient fermentative bacteria, such as Streptococcus pyogenes (206) and Streptococcus mutans (207).
Aifm2, a NADH Oxidase, Supports Robust Glycolysis and Is ...
After ISO, NADH oxidase activity in mitoplasts of Aifm2-transfected cells was higher by 10-fold compared to control cells. NADH oxidase activity of solubilized mitoplasts increased by only 1.5-fold, probably due to the presence of high NADH oxidase activity from complex I and III of ETC (data not shown).
Catalyzes the four-electron reduction of molecular oxygen to water. Active on beta-NADH, but not on alpha-NADH, beta-NADPH or alpha-NADPH. Under aerobic conditions, oxygen acts as the electron acceptor. Under anaerobic conditions, DCIP and MB can replace oxygen as the electron acceptor.