• Nitrate Reductase (NADH)" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
  • This graph shows the total number of publications written about "Nitrate Reductase (NADH)" by people in this website by year, and whether "Nitrate Reductase (NADH)" was a major or minor topic of these publications. (uchicago.edu)
  • Below are the most recent publications written about "Nitrate Reductase (NADH)" by people in Profiles. (uchicago.edu)
  • Reducing equivalents (NADH, FADH 2 ) are generated by reactions catalysed by the PDC and the tricarboxylic acid cycle and donate electrons (e - ) that enter the respiratory chain at NADH ubiquinone oxidoreductase (complex I) or at succinate ubiquinone oxidoreductase (complex II). (bmj.com)
  • Lipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.6.4.3) isolate from pig heart and Escherichia coli was covalently coupled by both diazonium and amide bonds to controlled pore glass beads (96% silica). (lvhn.org)
  • Dihydrolipoamide dehydrogenase (DLD), also known as dihydrolipoyl dehydrogenase, mitochondrial, is an enzyme that in humans is encoded by the DLD gene. (wikipedia.org)
  • The BCKD enzyme is a multimeric enzyme complex with four components, branched-chain keto acid decarboxylase alpha and beta subunits (E1 α and E1 β ), dihydrolipoyl transacylase (E2) subunit, and dihydrolipoamide dehydrogenase (E3) subunit. (nature.com)
  • In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. (expasy.org)
  • DLDH_CANFA Dihydrolipoyl dehydrogenase, mit. (nig.ac.jp)
  • DLDH_MOUSE Dihydrolipoyl dehydrogenase, mit. (nig.ac.jp)
  • DLHD_MANSE Dihydrolipoyl dehydrogenase (Dih. (nig.ac.jp)
  • DLDH_PEA Dihydrolipoyl dehydrogenase, mito. (nig.ac.jp)
  • DLD also has diaphorase activity, being able to catalyze the oxidation of NADH to NAD+ by using different electron acceptors such as O2, labile ferric iron, nitric oxide, and ubiquinone. (wikipedia.org)
  • Acidification of the mitochondrial matrix, as a result of ischemia-reperfusion injury, can disrupt the quaternary structure of DLD leading to decreased dehydrogenase activity and increased diaphorase activity. (wikipedia.org)
  • This enhancement in oxidative potential was shown to occur in all fiber types (NADH-diaphorase staining). (nih.gov)
  • We establish and characterize the Bckdha ( branched chain keto acid dehydrogenase a ) −/− mouse that exhibits a lethal neonatal phenotype mimicking human MSUD. (nature.com)
  • In these complexes, DLD converts dihydrolipoic acid and NAD+ into lipoic acid and NADH. (wikipedia.org)
  • DLD is a flavoprotein enzyme that oxidizes dihydrolipoamide to lipoamide. (wikipedia.org)
  • Dihydrolipoamide dehydrogenase (DLD) is a mitochondrial enzyme that plays a vital role in energy metabolism in eukaryotes. (wikipedia.org)
  • Lipoamide Dihydrolipoamide The protein encoded by the DLD gene comes together with another protein to form a dimer in the central metabolic pathway. (wikipedia.org)
  • DLD deficiency manifests itself in a great degree of variability, which has been attributed to varying effects of different DLD mutations on the stability of the protein and its ability to dimerize or interact with other components of the three α-ketoacid dehydrogenase complexes. (wikipedia.org)
  • The L protein, also named dihydrolipoamide dehydrogenase, is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. (thermofisher.com)
  • protein_coding" "AAC74323","adhE","Escherichia coli","fused acetaldehyde-CoA dehydrogenase/iron-dependent alcohol dehydrogenase/pyruvate-formate lyase deactivase [Ensembl]. (ntu.edu.sg)
  • The DLD homodimer functions as the E3 component of the pyruvate, α-ketoglutarate, α-adipate and branched-chain amino acid-dehydrogenase complexes and the glycine cleavage system, all in the mitochondrial matrix. (wikipedia.org)
  • Pyruvate may be reduced to lactate in the cytoplasm or may be transported into the mitochondria for anabolic reactions, such as gluconeogenesis and lipogenesis, or for oxidation to acetyl CoA by the pyruvate dehydrogenase (PDH) complex (PDC). (bmj.com)
  • The cycle of reaction is completed when reduced lipoamide is reoxidised by the flavoprotein, dihydrolipoamide dehydrogenase (E 3 ). (bmj.com)
  • Finally, the reduced flavoprotein is oxidised by NAD and transfers reducing equivalents to the respiratory chain via NADH. (bmj.com)
  • Under conditions in which oxygen supply is limiting, e.g., in exercising muscle, or in the absence of mitochondria, e.g., in red blood cells, re-oxidation of NADH produced by glycolysis cannot be coupled to generation of ATP. (reactome.org)
  • Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency. (thermofisher.com)
  • short chain dehydrogenase [Interproscan]. (ntu.edu.sg)
  • Glyceraldehyde 3-phosphate dehydrogenase [Interproscan]. (ntu.edu.sg)
  • The pyruvate dehydrogenase (PDH) multienzyme complex (PDC). (bmj.com)
  • A component of the multienzyme 2-oxo-acid dehydrogenase complexes. (expasy.org)
  • putative dihydrolipoamide dehydrogena. (nig.ac.jp)
  • putative dihydrolipoamide dehydroge. (nig.ac.jp)
  • The dihyrolipamide dehydrogenase gene is known to have multiple splice variants. (wikipedia.org)
  • Increases in the intramitochondrial ratios of NADH/NAD and acetyl CoA/CoA also stimulate kinase mediated phosphorylation of PDC. (bmj.com)
  • Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. (wikipedia.org)
  • The resulting hydroxyethyl-TPP complex reacts with oxidised lipoamide (LipS 2 ), the prosthetic group of dihydrolipoamide transacetylase (E 2 ), to form acetyl lipoamide. (bmj.com)
  • PYRUVATE DEHYDROGENASE ( LIPOAMIDE )- PHOSPHATASE catalyzes reactivation of the complex. (nih.gov)
  • It can be converted by the pyruvate dehydrogenase complex to acetyl CoA (Reed and Hackert 1990) which can enter the TCA cycle or serve as the starting point for the syntheses of long chain fatty acids, steroids, and ketone bodies depending on the tissue and metabolic state in which it is formed. (reactome.org)
  • These include beta-hydroxybutyrate dehydrogenase and acetoacetyl coenzyme A (CoA) synthetase (see the image below). (medscape.com)