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Pyruvate Dehydrogenase ComplexDihydrolipoamide DehydrogenasePyruvate Dehydrogenase (Lipoamide)Pyruvate Dehydrogenase (Lipoamide)-PhosphataseDihydrolipoyllysine-Residue AcetyltransferasePyruvate Dehydrogenase Complex Deficiency DiseaseKetoglutarate Dehydrogenase ComplexPyruvatesThioctic AcidPyruvic AcidPyruvate KinaseKetone OxidoreductasesDichloroacetic AcidThiamine PyrophosphateL-Lactate DehydrogenasePyruvate DecarboxylaseNAD3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)Alcohol DehydrogenaseGlycine Dehydrogenase (Decarboxylating)Glyceraldehyde-3-Phosphate DehydrogenasesGlycine Decarboxylase ComplexPyruvate OxidaseMalate DehydrogenaseAcetyltransferasesKineticsGlutamate DehydrogenaseIsocitrate DehydrogenaseStarvationCitric Acid CycleGlucosephosphate DehydrogenaseAldehyde DehydrogenaseOxidation-ReductionAzotobacterMolecular Sequence DataAcetyl Coenzyme AAmino Acid SequenceEscherichia coliMitochondriaGlucoseSuccinate DehydrogenaseAlcohol OxidoreductasesGeobacillus stearothermophilusCoenzyme AGlycolysisCarbohydrate DehydrogenasesLactic AcidL-Iditol 2-DehydrogenaseLactatesMultienzyme ComplexesMyocardiumOxidoreductasesProtein KinasesAzotobacter vinelandiiKetoglutaric AcidsGlycerolphosphate DehydrogenaseFlavin-Adenine DinucleotideNADPGlycine Decarboxylase Complex H-ProteinMalatesCaprylatesDecarboxylationSwineBinding SitesGlucose 1-DehydrogenaseLiverAldehyde OxidoreductasesIsoenzymesBase SequenceHydroxysteroid DehydrogenasesProtein-Serine-Threonine KinasesGlutathione ReductaseCloning, MolecularLiver Cirrhosis, BiliaryMitochondria, LiverAcidosis, LacticLactate DehydrogenasesPhosphogluconate DehydrogenaseAdenosine TriphosphateAcetatesKeto AcidsApoenzymesPyruvate CarboxylaseGlucose Dehydrogenases3-Hydroxysteroid DehydrogenasesNADH DehydrogenaseSugar Alcohol DehydrogenasesAcetylcarnitineAcetoacetatesAcyl-CoA DehydrogenasesHydrogen-Ion ConcentrationIMP DehydrogenaseSubstrate SpecificityOxygen ConsumptionMitochondria, HeartMitochondria, MuscleAurothioglucoseFormate DehydrogenasesCitrate (si)-SynthaseSpectrophotometry

PhosphataseDepressing pyruvate dehydrogenase coEnzymeDecarboxylaseDihydrolipoamide dehydrogenaseKinase isozymeOxidationOxidativeEnzymesNADHSubunitMultienzymeLactateThiamine pyrophosphateDeficiencyMetabolismProsthetic groupTricarboxylic acidGlucoseCoenzymeMutationsGlycolysisCellularRegulationGenesReactionAerobicComponentsConversionAmount

Phosphatase3

• Link to all annotated objects annotated to mitochondrial pyruvate dehydrogenase (lipoamide) phosphatase complex. (planteome.org)
• Link to all direct and indirect annotations to mitochondrial pyruvate dehydrogenase (lipoamide) phosphatase complex. (planteome.org)
• PYRUVATE DEHYDROGENASE ( LIPOAMIDE )- PHOSPHATASE catalyzes reactivation of the complex. (nih.gov)

Depressing pyruvate dehydrogenase co1

• Upregulation of MCUb limits mitochondrial matrix Ca 2+ uptake and impairs mitochondrial energy production via glucose oxidation by depressing pyruvate dehydrogenase complex activity. (diabetesjournals.org)

Enzyme6

• Pyruvate dehydrogenase (lipoamide) beta, also known as pyruvate dehydrogenase E1 component subunit beta, mitochondrial or PDHE1-B is an enzyme that in humans is encoded by the PDHB gene. (wikipedia.org)
• This gene provides instructions for making an enzyme called dihydrolipoamide dehydrogenase (DLD). (medlineplus.gov)
• DLD is one component of three different groups of enzymes that work together (enzyme complexes): branched-chain alpha-keto acid dehydrogenase (BCKD), pyruvate dehydrogenase (PDH), and alpha (α)-ketoglutarate dehydrogenase (αKGDH). (medlineplus.gov)
• The PDH complex also known as the pyruvate dehydrogenase complex is a multi-enzyme complex. (biotechfront.com)
• It is found, after its distribution to the various body tissues, intracellularly, intramitochondrialy and extracellularly.Metabolism: Alpha-lipoic acid is metabolized to its reduced form, dihydrolipoic acid (DHLA), by mitochondrial lipoamide dehydrogenase enzyme. (medicineindia.org)
• Pyruvate dehydrogenase (PDH) is an enzyme complex that catalyzes the conversion of pyruvate into acetyl-coA in vivo. (biomedcentral.com)

Decarboxylase2

• and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. (nih.gov)
• An essential cofactor of Pyruvate decarboxylase. (flashcardmachine.com)

Dihydrolipoamide dehydrogenase9

• Dihydrolipoamide dehydrogenase deficiency is a severe condition that can affect several body systems. (medlineplus.gov)
• A common feature of dihydrolipoamide dehydrogenase deficiency is a potentially life-threatening buildup of lactic acid in tissues (lactic acidosis), which can cause nausea, vomiting, severe breathing problems, and an abnormal heartbeat. (medlineplus.gov)
• Liver problems can also occur in dihydrolipoamide dehydrogenase deficiency, ranging from an enlarged liver (hepatomegaly) to life-threatening liver failure. (medlineplus.gov)
• Typically, the signs and symptoms of dihydrolipoamide dehydrogenase deficiency occur in episodes that may be triggered by fever, injury, or other stresses on the body. (medlineplus.gov)
• Dihydrolipoamide dehydrogenase deficiency occurs in an estimated 1 in 35,000 to 48,000 individuals of Ashkenazi Jewish descent. (medlineplus.gov)
• In other populations, the prevalence of dihydrolipoamide dehydrogenase deficiency is unknown, but the condition is likely rare. (medlineplus.gov)
• Mutations in the DLD gene cause dihydrolipoamide dehydrogenase deficiency. (medlineplus.gov)
• The brain is especially affected by the buildup of molecules and the lack of cellular energy, resulting in the neurological problems associated with dihydrolipoamide dehydrogenase deficiency. (medlineplus.gov)
• The cycle of reaction is completed when reduced lipoamide is reoxidised by the flavoprotein, dihydrolipoamide dehydrogenase (E 3 ). (bmj.com)

Kinase isozyme1

• Many scientific investigations have reported that Glucose transporter 8 (GLUT8), Adiponectin (ADIPOQ), Adiponectin receptor 1 (ADIPOR1), and Pyruvate dehydrogenase lipoamide kinase isozyme 4 (PDK4) show evidence that these genes contribute to mechanisms of fat deposition. (tnstate.edu)

Oxidation3

• Investigation of the mitochondrial energy metabolism showed reduced oxidation of pyruvate and decreased pyruvate dehydrogenase complex activity. (mpg.de)
• The oxidation of pyruvate to acetyl coenzyme A is an irreversible reaction . (biotechfront.com)
• 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)

Oxidative5

• The pyruvate dehydrogenase complex is responsible for the oxidative decarboxylation of pyruvate, with the final product being Acetyl CoA. (wikipedia.org)
• Lipoic acid is an essential prosthetic group of four mitochondrial enzymes involved in the oxidative decarboxylation of pyruvate, α-ketoglutarate, and branched chain amino acids and in the glycine cleavage. (mpg.de)
• Note that the oxidative fate of pyruvate is to be irreversibly decarboxylated to acetyl CoA. (bmj.com)
• Pathways of pyruvate metabolism and oxidative phosphorylation. (bmj.com)
• It is also metabolized to lipoamide, which functions as the lipoic acid cofactor in the multienzyme complexes that catalyze the oxidative decarboxylations of pyruvate and alpha-ketoglutarate. (medicineindia.org)

Enzymes3

• By this way in arsenic poisoning enzymes of the pyruvate dehydrogenase complex and alpha-keto glutarate complex are inhibited by arsenite. (biotechfront.com)
• Most identifiable cases involve inherited or spontaneous mutations in the pyruvate dehydrogenase complex (PDC) or in one or more enzymes of the respiratory chain. (bmj.com)
• 2 4 A few cases have been reported that involve deficiencies in enzymes of the tricarboxylic acid cycle, such as fumarase, or of gluconeogenesis, such as pyruvate carboxylase (PC) or phosphoenolpyruvate carboxykinase (PEPCK). (bmj.com)

NADH2

• PDH kinase which are responsible for the inactive PDH is promoted by ATP, NADH and acetyl coenzyme A. while PDH complex is inhibited by NAD+, coenzyme A and pyruvate. (biotechfront.com)
• Question: Including The Conversion Of Pyruvate To Acetyl CoA, How Many NADH, FADH2, ATP, And GTP Molecules Are Produced During The Kreb's Cycle? (nyxnews.com)

Subunit2

• A mitochondrial complex of a regulatory and catalytic subunit that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. (planteome.org)
• Pyruvate is decarboxylated by the PDH subunit (E 1 ) in the presence of thiamin pyrophosphate (TPP). (bmj.com)

Multienzyme4

• The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle. (wikipedia.org)
• The PDHB gene encodes a precursor protein that has 359 amino acid residues and a final mature protein that has 329 amino acids, and is part of the pyruvate dehydrogenase multienzyme complex. (wikipedia.org)
• A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. (nih.gov)
• The pyruvate dehydrogenase (PDH) multienzyme complex (PDC). (bmj.com)

Lactate1

• Under aerobic conditions, the activity of PDC determines the rate at which all cells oxidise glucose, pyruvate, and lactate. (bmj.com)

Thiamine pyrophosphate3

• Overall the complex catalyzes five reactions, with the overall reaction being: Pyruvate + CoA + NAD+ → acetyl-CoA + CO2 There are three different coenzymes required throughout the 5 steps that this complex carries out: thiamine pyrophosphate (TPP), lipoamide, and coenzyme A. This step is only one of the central metabolic pathway carried out by eukaryotes, in which glucose is oxidized to form carbon dioxide, water, and ATP. (wikipedia.org)
• Pyruvate Dehydrogenase with TPP as coenzyme, decarboxylates pyruvate to Hydroxyethyl TPP (thiamine pyrophosphate). (biotechfront.com)
• Then Dihydrolipoyl Transacetylase catalyzes conversion of Hydroxyethyl Thiamine Pyrophosphate into acetyl lipoamide and then transfers the acetyl group to coenzyme A to produce acetyl coenzyme A. (biotechfront.com)

Deficiency5

• Mutations in this gene are associated with pyruvate dehydrogenase E1-beta deficiency. (wikipedia.org)
• Mutations in the PDHB gene have been known to cause one form of pyruvate dehydrogenase deficiency. (wikipedia.org)
• Pyruvate dehydrogenase deficiency is characterized by the buildup of a chemical called lactic acid in the body and a variety of neurological problems. (wikipedia.org)
• People with pyruvate dehydrogenase deficiency usually have neurological problems as well. (wikipedia.org)
• Inherited or acquired alcoholics deficiency of PDH causes lactic acidosis due to rapid conversion of accumulated pyruvate into lactic acid. (biotechfront.com)

Metabolism1

• Serine/threonine kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. (thermofisher.com)

Prosthetic group2

• A pronounced reduction of the prosthetic group lipoamide was found in lipoylated proteins. (mpg.de)
• 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)

Tricarboxylic acid2

• This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. (thermofisher.com)
• Through a series of chemical reactions of pyruvate decarboxylation, the glycolytic pathway (the final product is pyruvate) and the tricarboxylic acid cycle (the initial reactant is acetyl-coA) can be effectively connected [ 7 ]. (biomedcentral.com)

Glucose1

• As a whole five ATP are released in the PDH complex and from two moles of pyruvate which is formed from glucose by glycolysis . (biotechfront.com)

Coenzyme4

• The E1 complex specifically uses the TPP cofactor to cleave the Calpha-C(=O) bond of pyruvate, and then transfer the acetyl group to the TPP coenzyme, thus resulting in an intermediate, hydroxylethyl-Tpp*E1, and producing CO2. (wikipedia.org)
• These include beta-hydroxybutyrate dehydrogenase and acetoacetyl coenzyme A (CoA) synthetase (see the image below). (medscape.com)
• In the mitochondrial matrix pyruvate is oxidatively Decarboxylated to form Acetyl- CoA (acetyl coenzyme A). (biotechfront.com)
• In turn, this intermediate reacts with reduced coenzyme A (CoASH) to yield acetyl CoA and reduced lipoamide (Lip(SH) 2 ). (bmj.com)

Mutations1

• Mutations in this gene are associated with pyruvate dehydrogenase E1-alphadeficiency and X-linked Leigh syndrome. (researchtoactionforum.org)

Glycolysis2

• Pyruvate is produced in the cytosol as the end product of aerobic glycolysis . (biotechfront.com)
• Pyruvate kinase regulation is important for controlling the flux of metabolites, such as fructose (in liver), which enter glycolysis after the PFK step. (flashcardmachine.com)

Cellular1

• These data suggest that following nutrient restriction, the structural integrity of the rumen wall is compromised and there is upregulation of genes involved in the production of ketone bodies and breakdown of pyruvate for cellular energy. (biomedcentral.com)

Regulation1

• Regulation of the pyruvate dehydrogenase complex is mainly an example of end product inhibition. (biotechfront.com)

Genes1

• Also, housekeeping genes Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and 18s ribosomal RNA (18s rRNA) were assayed to determine which one is more constant in abdominal fat tissue. (tnstate.edu)

Reaction1

• What is the metabolic importance of regulating flux through the pyruvate kinase reaction? (flashcardmachine.com)

Aerobic1

• Under aerobic conditions pyruvate is oxidized into? (flashcardmachine.com)

Components1

• The PDH complex is composed of multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). (wikipedia.org)

Conversion1

• Dihydrolipoyl Dehydrogenase catalyses conversion of reduced Lipamind into Oxidized lipamind by transferring the reduced equivalence of FAD and this completes the cycle. (biotechfront.com)

Amount1

• The pyruvate dehydrogenase complex is turned off because when enough amount of ATP is already present there is no need for the pyruvate dehydrogenase complex to continue. (biotechfront.com)