Dihydrolipoamide dehydrogenasePyruvate dehydroLipoic acidMitochondrialSubunitLeucineOxidoreductaseSubstrateLipoylOxidativeLipoamideReactionEnzyme complexKrebsSynthaseAcidSubunitsProteinGrowthFormEnergyRoleStructureProcessPyruvate dehydrogenaseChain ketoacidOxidative decarboxylationBranched-chainThiamineCatalyticEnzymaticMapleBetaPreventsEssentialForms
Dihydrolipoamide dehydrogenase2
- This enzyme complex is composed of three catalytic components: alpha-ketoacid dehydrogenase (also referred to as the E1 component), dihydrolipoyl transacylase (E2 component), and dihydrolipoamide dehydrogenase (E3 component). (wikipedia.org)
- The cycle of reaction is completed when reduced lipoamide is reoxidised by the flavoprotein, dihydrolipoamide dehydrogenase (E 3 ). (bmj.com)
Pyruvate dehydro2
- 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)
- 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)
Lipoic acid12
- Alpha-lipoic acid is a nutritional coenzyme that is involved in energy metabolism of proteins, carbohydrates and fats, has physiological functions in blood glucose disposal, and is able to scavenge a number of free radicals. (drguberman.com)
- Alpha-Lipoic Acid (100mg) 60t is available by Douglas Laboratories. (drguberman.com)
- Alpha-Lipoic Acid tablets, provided by Douglas Laboratories, contain 100 mg of pure alpha-lipoic acid. (drguberman.com)
- Alpha-lipoic acid is a non-vitamin coenzyme that carries out important metabolic and antioxidant functions in the body. (drguberman.com)
- Alpha-lipoic acid may be a beneficial dietary supplement for those concerned about a more complete antioxidant defense system and maintaining proper glucose metabolism. (drguberman.com)
- Dietary and supplementary alpha-lipoic acid is efficiently absorbed, transported to the tissues, and readily taken up by the cells. (drguberman.com)
- Alpha-lipoic acid is a fat- and water-soluble, sulfurcontaining coenzyme. (drguberman.com)
- As part of several multi-enzyme complexes located in the mitochondria, alpha-lipoic acid is essential for metabolizing carbohydrates, proteins, and fats, and for the conversion of their energy into ATP. (drguberman.com)
- Another lipoic acid containing enzyme complex, BCKADH (branched-chain keto-acid dehydrogenase), is involved in deriving energy from the branched chain amino acids, leucine, isoleucine, and valine. (drguberman.com)
- A related metabolic function of alpha-lipoic acid is its role in blood glucose disposal. (drguberman.com)
- As early as 1959, alpha-lipoic acid was suggested to be an antioxidant, since it could extend the actions of vitamin C in guinea pigs, and those of vitamin E in rats. (drguberman.com)
- It is only recently, however, that the specific actions of alpha-lipoic acid in free radical quenching, metal chelation, and antioxidant regeneration have been investigated. (drguberman.com)
Mitochondrial3
- The branched-chain α-ketoacid dehydrogenase complex (BCKDC or BCKDH complex) is a multi-subunit complex of enzymes that is found on the mitochondrial inner membrane. (wikipedia.org)
- BCKDC is a member of the mitochondrial α-ketoacid dehydrogenase complex family comprising pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, key enzymes that function in the Krebs cycle. (wikipedia.org)
- The genes of the alpha and beta subunits of the mitochondrial trifunctional protein are located adjacent to each other in the human genome in a head-to-head orientation. (wikidoc.org)
Subunit2
- A full-length cDNA (Ov-phy-1) encoding a catalytically active alpha-subunit of Onchocerca volvulus prolyl 4-hydroxylase was isolated and characterized. (embl.de)
- This control is propagated through the alpha-subunit of prolyl 4-hydroxylase where protein levels were previously shown to rise fivefold with increasing cell density. (embl.de)
Leucine2
- Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+. (lookformedical.com)
- An enzyme that catalyzes the first step in the biosynthetic pathway to LEUCINE , forming isopropyl malate from acetyl-CoA and alpha-ketoisovaleric acid. (lookformedical.com)
Oxidoreductase1
- 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)
Substrate1
- 1. O'Connor, R.J. and Halvorson, H. The substrate specificity of L -alanine dehydrogenase. (qmul.ac.uk)
Lipoyl1
- E1 catalyzes both the decarboxylation of the α-ketoacid and the subsequent reductive acylation of the lipoyl moiety (another catalytic cofactor) that is covalently bound to E2. (wikipedia.org)
Oxidative1
- This enzyme complex catalyzes the oxidative decarboxylation of branched, short-chain alpha-ketoacids. (wikipedia.org)
Lipoamide1
- 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)
Reaction1
- The inner-core domain is necessary to form the oligomeric core of the enzyme complex and catalyzes the acyltransferase reaction (shown in the "Mechanism" section below). (wikipedia.org)
Enzyme complex1
- The mechanism of enzymatic catalysis by the BCKDC draws largely upon the elaborate structure of this large enzyme complex. (wikipedia.org)
Krebs1
- Two of these enzyme complexes, PDH (pyruvate dehydrogenase) and alpha-KGDH (alpha-ketoglutarate dehydrogenase) are part of the citric acid cycle (Krebs cycle), and as such assume a central role for general energy production. (drguberman.com)
Synthase1
- Cytochrome c oxidase (complex IV) catalyses the reduction of molecular oxygen to water and ATP synthase (complex V) generates ATP from ADP. (bmj.com)
Acid3
- A component of the multienzyme 2-oxo-acid dehydrogenase complexes. (expasy.org)
- 1. Olson, J.A. and Anfinsen, C.B. The crystallization and characterization of L -glutamic acid dehydrogenase. (qmul.ac.uk)
- An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. (lookformedical.com)
Subunits2
- Twenty alpha-amino acids are the subunits which are polymerized to form proteins . (lookformedical.com)
- Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. (lookformedical.com)
Protein1
- [4] Trifunctional protein deficiency is characterized by decreased activity of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), long-chain enoyl-CoA hydratase, and long-chain thiolase. (wikidoc.org)
Growth1
- Anabolism is the formation and storage of complex compounds needed for growth, tissue repair and energy storage from simpler molecules. (oncohemakey.com)
Form1
- DNA-binding motifs formed from two alpha-helixes which intertwine for about eight turns into a coiled coil and then bifurcate to form Y shaped structures. (lookformedical.com)
Energy1
- Catabolism is the breakdown of large complex molecules to provide energy for cellular activity and smaller compounds, e.g. amino acids, needed for anabolic reactions or for elimination from the body. (oncohemakey.com)
Role2
- This may be explained by its functions in the glucosemetabolizing enzymes, PDH and alpha-KGDH, but some researchers suspect a more direct role in cellular glucose uptake at the cell membrane. (drguberman.com)
- It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes. (expasy.org)
Structure1
- However, due to the complex and recalcitrant structure of plant cell walls, the process of regenerating these feedstocks are usually complex resulting the high cost. (researchsquare.com)
Process1
- Lipid transport is a complex process and is discussed in Chapter 19. (oncohemakey.com)
Pyruvate dehydrogenase6
- BCKDC is a member of the mitochondrial α-ketoacid dehydrogenase complex family comprising pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, key enzymes that function in the Krebs cycle. (wikipedia.org)
- It is composed of 3 subunits designated as E1, E2, and E3 and is a member of the short chain oxo-acid dehydrogenase family along with pyruvate dehydrogenase and 2- oxoglutarate dehydrogenase. (aacc.org)
- Pantothenic acid (B5) is required for coenzyme A formation and is also essential for alpha-ketoglutarate and pyruvate dehydrogenase complexes as well as fatty acid oxidation. (nih.gov)
- We report the crystal structures of the phosporylated pyruvate dehydrogenase (E1p) component of the human pyruvate dehydrogenase complex (PDC). (nih.gov)
- The complete phosphorylation at Ser264-alpha (site 1) of a variant E1p protein was achieved using robust pyruvate dehydrogenase kinase 4 free of the PDC core. (nih.gov)
- In its diphosphate form (also known as TDP, thiamine pyrophosphate, TPP, or cocarboxylase), it serves as a cofactor for enzymes involved in carbohydrate metabolism, including transketolase, α-ketoglutarate dehydrogenase, pyruvate dehydrogenase, and branched chain α-keto acid dehydrogenase. (ferienwohnung-gluecksburg.net)
Chain ketoacid3
- Next, the branched chain-2-oxoacids undergo irreversible oxidative decarboxylation in the mitochondria catalyzed by the branched-chain ketoacid dehydrogenase complex (BCKDHc). (aacc.org)
- Defects in the branched chain ketoacid dehydrogenase complex are responsible for maple syrup urine disease. (aacc.org)
- Thiamin (B1) is essential for the oxidative decarboxylation of the multienzyme branched-chain ketoacid dehydrogenase complexes of the citric acid cycle. (nih.gov)
Oxidative decarboxylation2
- This enzyme complex catalyzes the oxidative decarboxylation of branched, short-chain alpha-ketoacids. (wikipedia.org)
- The E1 subunit of the complex is responsible for the oxidative decarboxylation of 2-oxoacids and requires thiamin pyrophosphate as a co-factor. (aacc.org)
Branched-chain4
- In order to obtain insight into the effect of mutations observed in MSUD patients, we determined the crystal structure of branched-chain alpha-ketoacid dehydrogenase (E1), the 170 kDa alpha(2)beta(2) heterotetrameric E1b component of the branched-chain alpha-ketoacid dehydrogenase multienzyme complex. (rcsb.org)
- The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). (nih.gov)
- It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). (nih.gov)
- This enzyme complex functions in the catabolism of branched-chain amino acids. (nih.gov)
Thiamine1
- We show that unlike its unmodified counterpart, the presence of a phosphoryl group at Ser264-alpha prevents the cofactor thiamine diphosphate-induced ordering of the two loops carrying the three phosphorylation sites. (nih.gov)
Catalytic1
- E1 catalyzes both the decarboxylation of the α-ketoacid and the subsequent reductive acylation of the lipoyl moiety (another catalytic cofactor) that is covalently bound to E2. (wikipedia.org)
Enzymatic1
- The latter components regulate enzymatic activity by interconverting the dehydrogenase between active (nonphosphorylated) and inactive (phosphorylated) forms involving three specific serine residues that participate in TPP binding. (ferienwohnung-gluecksburg.net)
Maple1
- Mutations in components of the extraordinarily large alpha-ketoacid dehydrogenase multienzyme complexes can lead to serious and often fatal disorders in humans, including maple syrup urine disease (MSUD). (rcsb.org)
Beta1
- It is composed of two subunits: E1 alpha and E1 beta. (aacc.org)
Prevents1
- It is likely that the enzyme stabilizes the TPP-acetaldehyde complex and prevents this condensation from occurring. (ferienwohnung-gluecksburg.net)
Essential1
- The disordering of these phosphorylation loops is caused by a previously unrecognized steric clash between the phosphoryl group at site 1 and a nearby Ser266-alpha, which nullifies a hydrogen-bonding network essential for maintaining the loop conformations. (nih.gov)
Forms1
- Firstly, the production of precursors such as amino acids , monosaccharides , isoprenoids and nucleotides , secondly, their activation into reactive forms using energy from ATP, and thirdly, the assembly of these precursors into complex molecules such as proteins , polysaccharides , lipids and nucleic acids . (medmuv.com)