Loading...
  • NADP
  • Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. (nih.gov)
  • Binding of the substrate 6-phospho-d-gluconate (6PG), the inhibitors 5-phospho-d-ribonate (5PR) and 4PE, and the coenzymes NADP, NADPH and NADP analogue 3-amino-pyridine adenine dinucleotide phosphate to 6-phospho-d-gluconate dehydrogenase from T. brucei was studied using isothermal titration calorimetry. (unife.it)
  • substrate
  • ADH3 (identical to glutathione-dependent formaldehyde dehydrogenase) is clearly the ancestral ADH form and S-hydroxymethylglutathione is the main physiological substrate, but the enzyme can still oxidize ethanol at high concentrations. (springer.com)
  • enzymology
  • In enzymology, a D-2-hydroxy-acid dehydrogenase (EC 1.1.99.6) is an enzyme that catalyzes the chemical reaction (R)-lactate + acceptor ⇌ {\displaystyle \rightleftharpoons } pyruvate + reduced acceptor Thus, the two substrates of this enzyme are (R)-lactate and acceptor, whereas its two products are pyruvate and reduced acceptor. (wikipedia.org)
  • In enzymology, a spermidine dehydrogenase (EC 1.5.99.6) is an enzyme that catalyzes the chemical reaction spermidine + acceptor + H2O ⇌ {\displaystyle \rightleftharpoons } propane-1,3-diamine + 4-aminobutanal + reduced acceptor The 3 substrates of this enzyme are spermidine, acceptor, and H2O, whereas its 3 products are propane-1,3-diamine, 4-aminobutanal, and reduced acceptor. (wikipedia.org)
  • In enzymology, a phenylacetaldehyde dehydrogenase (EC 1.2.1.39) is an enzyme that catalyzes the chemical reaction phenylacetaldehyde + NAD+ + H2O ⇌ {\displaystyle \rightleftharpoons } phenylacetate + NADH + 2 H+ The 3 substrates of this enzyme are phenylacetaldehyde, NAD+, and H2O, whereas its 3 products are phenylacetate, NADH, and H+. (wikipedia.org)
  • In enzymology, a cytokinin dehydrogenase (EC 1.5.99.12) is an enzyme that catalyzes the chemical reaction N6-dimethylallyladenine + electron acceptor + H2O ⇌ {\displaystyle \rightleftharpoons } adenine + 3-methylbut-2-enal + reduced acceptor The 3 substrates of this enzyme are cytokinin (here represented by N6-dimethylallyladenine), electron acceptor, and H2O, whereas its 3 products are adenine, 3-methylbut-2-enal (or other aldehyde in case of different substrate), and reduced acceptor. (wikipedia.org)
  • In enzymology, a phenylalanine dehydrogenase (EC 1.4.1.20) is an enzyme that catalyzes the chemical reaction L-phenylalanine + H2O + NAD+ ⇌ {\displaystyle \rightleftharpoons } phenylpyruvate + NH3 + NADH + H+ The 3 substrates of this enzyme are L-phenylalanine, H2O, and NAD+, whereas its 4 products are phenylpyruvate, NH3, NADH, and H+. (wikipedia.org)
  • In enzymology, a choline dehydrogenase (EC 1.1.99.1) is an enzyme that catalyzes the chemical reaction choline + acceptor ⇌ {\displaystyle \rightleftharpoons } betaine aldehyde + reduced acceptor Thus, the two substrates of this enzyme are choline and acceptor, whereas its two products are betaine aldehyde and reduced acceptor. (wikipedia.org)
  • In enzymology, an ureidoglycolate dehydrogenase (EC 1.1.1.154) is an enzyme that catalyzes the chemical reaction (S)-ureidoglycolate + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } oxalureate + NAD(P)H + H+ The 3 substrates of this enzyme are (S)-ureidoglycolate, NAD+, and NADP+, whereas its 4 products are oxalureate, NADH, NADPH, and H+. (wikipedia.org)
  • electrons
  • NADH dehydrogenase ( EC 1.6.5.3 ) (also referred to as "NADH:quinone reductase" or "Complex I") is an enzyme located in the inner mitochondrial membrane that catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). (princeton.edu)
  • NADH initially binds to NADH dehydrogenase, and transfers two electrons to the flavin mononucleotide (FMN) prosthetic group of complex I, creating FMNH 2 . (princeton.edu)
  • The electrons are then transferred through the second prosthetic group of NADH dehydrogenase via a series of iron-sulfur (Fe-S) clusters, and finally to coenzyme Q (ubiquinone). (princeton.edu)
  • glutamate
  • Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. (wikipedia.org)
  • In humans the relevant genes are called GLUD1 (glutamate dehydrogenase 1) and GLUD2 (glutamate dehydrogenase 2), and there are also at least 8 GLDH pseudogenes in the human genome as well, probably reflecting microbial influences on eukaryote evolution. (wikipedia.org)
  • NAD+(or NADP+) is a cofactor for the glutamate dehydrogenase reaction, producing α-ketoglutarate and ammonium as a byproduct. (wikipedia.org)
  • In humans, the activity of glutamate dehydrogenase is controlled through ADP-ribosylation, a covalent modification carried out by the gene sirt4. (wikipedia.org)
  • Under these circumstances, glutamate dehydrogenase activity is raised in order to increase the amount of α-ketoglutarate produced, which can be used to provide energy by being used in the citric acid cycle to ultimately produce ATP. (wikipedia.org)
  • Mutations alter the allosteric binding site of GTP cause permanent activation of glutamate dehydrogenase lead to disorder known as hyperinsulinism-hyperammonemia. (wikipedia.org)
  • deficiency
  • Succinic semialdehyde dehydrogenase deficiency ( SSADHD ), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric aciduria , is a rare autosomal recessive disorder of the degradation pathway of the inhibitory neurotransmitter γ-aminobutyric acid , or GABA . (wikipedia.org)
  • However, because of the deficiency, the final intermediate of the GABA degradation pathway, succinic semialdehyde, accumulates and cannot be oxidized to succinic acid and is therefore reduced to gamma-hydroxybutyric acid (GHB) by gamma-hydroxybutyric dehydrogenase. (wikipedia.org)
  • Succinic semialdehyde dehydrogenase deficiency has an autosomal recessive pattern of inheritance. (wikipedia.org)
  • Deficiency in ETF dehydrogenase causes the human genetic disease multiple acyl-CoA dehydrogenase deficiency. (wikipedia.org)
  • Deficiency of ETF-QO results in a disorder known as glutaric acidemia type II (also known as MADD for multiple acyl-CoA dehydrogenase deficiency), in which there is an improper buildup of fats and proteins in the body. (wikipedia.org)
  • Dihyropyrimidine dehydrogenase deficiency shows large phenotypic variability, ranging from no symptoms to a convulsive disorder with motor and mental retardation in homozygous patients. (nih.gov)
  • oxidative
  • Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) and (EC 1.1.1.41) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. (wikipedia.org)