Other names in common use include reduced nicotinamide adenine dinucleotide (quinone) dehydrogenase, NADH-quinone oxidoreductase, NADH ubiquinone oxidoreductase, DPNH-menadione reductase, D-diaphorase, and NADH2 dehydrogenase (quinone), and mitochondrial (mt) complex I. This enzyme participates in oxidative phosphorylation. (wikipedia.org)
NADH dehydrogenase is involved in the first step of the electron transport chain of oxidative phosphorylation (OXPHOS). (wikipedia.org)
NADP1
FLAVOPROTEIN containing siroheme and can utilize both NAD and NADP as cofactors. (lookformedical.com)
Oxidase4
An NADPH oxidase that is strongly expressed in the kidney. (nih.gov)
A flavoprotein oxidase complex that contains iron-sulfur centers. (ouhsc.edu)
In line with these results, studies using various enzyme inhibitors, such as DPI, allopurinol, rotenone, N G -monomethyl- l -arginine, and indomethacin, suggest that the predominant source of superoxide anion in vascular particulate fraction is NADH-dependent membrane-bound oxidase. (diabetesjournals.org)
These findings suggest that upregulated expression of p22phox mRNA and enhanced NADH oxidase activity contribute to the impaired endothelium-dependent vasodilation in OLETF rats. (diabetesjournals.org)
Mitochondrial1
A mitochondrial flavoprotein, this enzyme catalyzes the oxidation of 3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA using FAD as a cofactor. (bvsalud.org)
Enzyme5
This enzyme catalyses the following chemical reaction: NADH + H+ + a quinone ⇌ {\displaystyle \rightleftharpoons } NAD+ + a quinol The 3 substrates of this enzyme are NADH, H+, and a quinone (electron acceptor), whereas its two products are NAD+ and a quinol (reduced acceptor). (wikipedia.org)
An important example of this reaction is: NADH + H+ + ubiquinone ⇌ {\displaystyle \rightleftharpoons } NAD+ + ubiquinol This enzyme is a flavoprotein (FAD). (wikipedia.org)
The systematic name of this enzyme class is NADH:(quinone-acceptor) oxidoreductase. (wikipedia.org)
The enzyme has a preference for NADPH as the reductant, with NADH being a poor substitute [2]. (enzyme-database.org)
Using NADPH and O 2 as cosubstrates, the enzyme inserts one atom of oxygen into the substrate in a complex catalytic mechanism that involves the formation of a flavin-peroxide and Criegee intermediate. (acs.org)
Quinone1
NAD(P)H:quinone acceptor oxidoreductase 1 (NQO1) is a widely-distributed FAD-dependent flavoprotein that promotes obligatory 2-electron reductions of quinones, quinoneimines, nitroaromatics, and azo dyes, at rates that are comparable with NADH or NADPH. (dundee.ac.uk)
Acceptor2
In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. (lookformedical.com)
The systematic name is based on donor:acceptor oxidoreductase. (lookformedical.com)
Fumarate1
Interaction with C4 dicarboxylic acids and identification of a novel L -aspartate: fumarate oxidoreductase activity. (enzyme-database.org)
Characterization1
1. Fischer, D., Ebenau-Jehle, C. and Grisebach, H. Phytoalexin synthesis in soybean: purification and characterization of NADPH:2'-hydroxydaidzein oxidoreductase from elicitor-challenged soybean cell cultures. (qmul.ac.uk)
Electron2
In the electron transport chain NADH is mainly used to create a concentration gradient of hydrogen in order to make ATP. (wikipedia.org)
Therefore, the current work utilizes three flavin analogues: riboflavin (RF), flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which differ in size and charge but have similar redox potentials, to relay electron from nicotinamide adenine dinucleotide (NADH) to ferritin mineral core. (bvsalud.org)
Substrate2
The production of superoxide anion in response to NADH as a substrate was markedly increased in the vascular homogenates, but NADPH, arachidonic acid, xanthine, and succinate produced only small increases in chemiluminescence. (diabetesjournals.org)
X-ray crystallography was used to investigate this complex enzymatic process, which showed Orf1 has two substrate-binding sites that sit 13.5 Å apart unlike canonical FAD-dependent oxidoreductases. (hokudai.ac.jp)
Hydroxylase2
Properties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum. (genome.jp)
Anthranilate hydroxylase from Aspergillus niger: new type of NADPH-linked nonheme iron monooxygenase. (genome.jp)
Flavin1
Smaller sized/neutral flavin analogue, riboflavin (RF) exhibits faster reactivity towards both NADH and O2 generating more amount of O2â - and releases higher amount of iron from different ferritins, compared to its larger sized/negatively charged derivatives such as FMN and FAD. (bvsalud.org)
Monooxygenase1
Cyclohexanone monooxygenase (CHMO) is a flavoprotein that carries out the archetypical Baeyer−Villiger oxidation of a variety of cyclic ketones into lactones. (acs.org)
Superoxide1
In the presence of NADH, deflavinization of flavoproteins leads to formation of superoxide by at least of three processes. (bvsalud.org)
Reduction1
Oxidoreductases that are specific for the reduction of NITRATES. (lookformedical.com)
Preference1
Growth-Based, High-Throughput Selection for NADH Preference in an Oxygen-Dependent Biocatalyst. (acs.org)
Activity1
In vitro kinetic assays on crude hktE - pgdx - H. influenzae Rd extracts revealed the presence of NAD(P)H:peroxide oxidoreductase activity, which, however, appears to be physiologically insignificant because of its low affinity for H 2 O 2 ( K m = 1.1 mM). (biomedcentral.com)
Acting1
It belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. (wikipedia.org)
Iron2
The initial step, i.e., interaction of flavins with NADH played critical role in the iron release process. (bvsalud.org)
Therefore, these structure-reactivity studies of flavins with NADH/O2 holds significance in ferritin iron release, bioenergetics, O2-based cellular toxicity and may be potentially exploited in the treatment of methemoglobinemia. (bvsalud.org)
Reductase activity1
This gene encodes a taxon-specific crystallin protein which has NADPH-dependent quinone reductase activity distinct from other known quinone reductases. (nih.gov)
Escherichia2
Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities. (nih.gov)
Two soluble flavoproteins, purified from Escherichia coli cytosol and identified as flavodoxin and NADPH-flavodoxin (ferredoxin) reductase (flavodoxin reductase), have been found in combination to support the 17 alpha-hydroxylase activities of heterologously expressed bovine 17 alpha-hydroxylase cytochrome P450 (P450c17). (nih.gov)
Gene1
Glutaric acidemia type II: gene structure and mutations of the electron transfer flavoprotein:ubiquinone oxidoreductase (ETF:QO) gene. (nih.gov)
Ferredoxin1
NADH-dependent reduced ferredoxin:NADP oxidoreductase (NfnAB) is found in the cytoplasm of various anaerobic bacteria and archaea. (nih.gov)
Substrates1
Cytochrome P450 enzymes use haem to oxidise their substrates, using protons derived from NADH or NADPH to split the oxygen so a single atom can be added to a substrate. (embl.de)
Protein2
Flavodoxin reductase, possessing FAD as a cofactor, is able to reconstitute P450c17 activities only in the presence of flavodoxin, an FMN-containing protein, and NAD(P)H. Reducing equivalents are utilized more effectively from NADPH than NADH by flavodoxin reductase. (nih.gov)
Most prokaryotes and mitochondria (and fungal CYP55) have 3-component systems (class I/class B) - a FAD-containing flavoprotein (NAD(P)H-dependent reductase), an iron-sulphur protein and P450. (embl.de)
Nitrate2
An iron-sulfur and MOLYBDENUM containing FLAVOPROTEIN that catalyzes the oxidation of nitrite to nitrate. (bvsalud.org)
It belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. (wikipedia.org)
Molecular1
Physical characteristics of the two flavoproteins including absorbance spectra, molecular weights, and amino-terminal sequences are identical with those reported previously for E. coli flavodoxin and flavodoxin reductase. (nih.gov)
Class1
Most eukaryotic microsomes have 2-component systems (class II/class E) - NADPH:P450 reductase (FAD and FMN-containing flavoprotein) and P450. (embl.de)
Presence1
is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. (nih.gov)
17. The Crystal Structures of Bacillithiol Disulfide Reductase Bdr (YpdA) Provide Structural and Functional Insight into a New Type of FAD-Containing NADPH-Dependent Oxidoreductase. (nih.gov)