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In mammals, NADPH oxidase is found in two types: one in white blood cells (neutrophilic) and the other in vascular cells, differing in biochemical structure and functions. [3] Neutrophilic NADPH oxidase produces superoxide almost instantaneously, whereas the vascular enzyme produces superoxide in minutes to hours. [4]
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 ...
EC 1.4 includes oxidoreductases that act on the CH-NH 2 group of donors (Amino acid oxidoreductases, Monoamine oxidase) EC 1.5 includes oxidoreductases that act on CH-NH group of donors; EC 1.6 includes oxidoreductases that act on NADH or NADPH; EC 1.7 includes oxidoreductases that act on other nitrogenous compounds as donors
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 ...
NADPH oxidase 2 (Nox2), also known as cytochrome b(558) subunit beta or Cytochrome b-245 heavy chain, is a protein that in humans is encoded by the NOX2 gene (also called CYBB gene). [5] The protein is a superoxide generating enzyme which forms reactive oxygen species (ROS).
In enzymology, a NADH peroxidase (EC 1.11.1.1) 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.
The systematic name of this enzyme class is L-proline:NAD(P)+ 5-oxidoreductase. Other names in common use include proline oxidase, L-proline oxidase, 1-pyrroline-5-carboxylate reductase, NADPH-L-Delta1-pyrroline carboxylic acid reductase, and L-proline-NAD(P)+ 5-oxidoreductase. This enzyme participates in arginine and proline metabolism.