2.02012-05-31 13:02:53 -06002015-09-13 15:15:20 -0600ECMDB00985M2MDB000215DihydrolipoamideDihydrolipoamide is a member of the chemical class known as N-acyl Amines. These are compounds containing a fatty acid moiety linked to an amine group through an ester linkage. Dihydrolipoamide is a molecule produced by the action of dihydrolipoyl dehydrogenase upon lipoamide.6,8-bis-sulfanyloctanamide6,8-Bis-sulphanyloctanamide6,8-dimercapto-Octanamide6,8-dimercaptooctanamide6,8-disulfanyloctanamide6,8-DisulphanyloctanamideDihydrolipoamideDihydrothioctamideC8H17NOS2207.357207.0751555516,8-disulfanyloctanimidic aciddihydrothioctamide3884-47-7OC(=N)CCCCC(S)CCSInChI=1S/C8H17NOS2/c9-8(10)4-2-1-3-7(12)5-6-11/h7,11-12H,1-6H2,(H2,9,10)VLYUGYAKYZETRF-UHFFFAOYSA-NOuter membraneInner membranelogp2.22logs-3.32solubility9.92e-02 g/llogp1.44pka_strongest_acidic6.68pka_strongest_basic8.78iupac6,8-disulfanyloctanimidic acidaverage_mass207.357mono_mass207.075155551smilesOC(=N)CCCCC(S)CCSformulaC8H17NOS2inchiInChI=1S/C8H17NOS2/c9-8(10)4-2-1-3-7(12)5-6-11/h7,11-12H,1-6H2,(H2,9,10)inchikeyVLYUGYAKYZETRF-UHFFFAOYSA-Npolar_surface_area44.08refractivity68.7polarizability23.77rotatable_bond_count7acceptor_count2donor_count4physiological_charge0formal_charge0glycolysis and pyruvate dehydrogenaseFructose metabolism begins with the transport of Beta-D-glucose 6-phosphate through a glucose PTS permease, resulting in a Beta-D-glucose 6-phosphate. This compound is isomerized by a glucose-6-phosphate isomerase resulting in a fructose 6-phosphate. This compound can be phosphorylated by two different enzymes, a pyridoxal phosphatase/fructose 1,6-bisphosphatase or a ATP driven-6-phosphofructokinase-1 resulting in a fructose 1,6-biphosphate. This compound can either react with a fructose bisphosphate aldolase class 1 resulting in D-glyceraldehyde 3-phosphate and a dihydroxyacetone phosphate or through a fructose biphosphate aldolase class 2 resulting in a D-glyceraldehyde 3-phosphate. This compound can then either react in a reversible triosephosphate isomerase resulting in a dihydroxyacetone phosphate or react with a phosphate through a NAD dependent Glyceraldehyde 3-phosphate dehydrogenase resulting in a glyceric acid 1,3-biphosphate. This compound is desphosphorylated by a phosphoglycerate kinase resulting in a 3-phosphoglyceric acid.This compound in turn can either react with a 2,3-bisphosphoglycerate-independent phosphoglycerate mutase or a 2,3-bisphosphoglycerate-independent phosphoglycerate mutase resulting in a 2-phospho-D-glyceric acid. This compound interacts with an enolase resulting in a phosphoenolpyruvic acid and water. Phosphoenolpyruvic acid can react either through a AMP driven phosphoenoylpyruvate synthase or a ADP driven pyruvate kinase protein complex resulting in a pyruvic acid.
Pyruvic acid reacts with CoA through a NAD driven pyruvate dehydrogenase complex resulting in a carbon dioxide and a Acetyl-CoA which gets incorporated into the TCA cycle pathway.
PW000785MetabolicSpecdb::CMs3275Specdb::CMs37877Specdb::CMs157098Specdb::CMs1083092Specdb::CMs1083093Specdb::CMs1083094Specdb::CMs1083095Specdb::CMs1083096Specdb::CMs1083097Specdb::CMs1083098Specdb::NmrOneD293955Specdb::NmrOneD293956Specdb::NmrOneD293957Specdb::NmrOneD293958Specdb::NmrOneD293959Specdb::NmrOneD293960Specdb::NmrOneD293961Specdb::NmrOneD293962Specdb::NmrOneD293963Specdb::NmrOneD293964Specdb::NmrOneD293965Specdb::NmrOneD293966Specdb::NmrOneD293967Specdb::NmrOneD293968Specdb::NmrOneD293969Specdb::NmrOneD293970Specdb::NmrOneD293971Specdb::NmrOneD293972Specdb::NmrOneD293973Specdb::NmrOneD293974Specdb::MsMs23009Specdb::MsMs23010Specdb::MsMs23011Specdb::MsMs29807Specdb::MsMs29808Specdb::MsMs29809Specdb::MsMs2712296Specdb::MsMs2712297Specdb::MsMs2712298Specdb::MsMs2996966Specdb::MsMs2996967Specdb::MsMs2996968HMDB00985643C0057917694DIHYDROLIPOAMIDEDihydrolipoamideKeseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.22080510van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25.17765195Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.18331064Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT: Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J Mol Biol. 2005 Jul 15;350(3):543-52.15946682Kim H: Asparagine-473 residue is important to the efficient function of human dihydrolipoamide dehydrogenase. J Biochem Mol Biol. 2005 Mar 31;38(2):248-52.15826505McMillan PJ, Stimmler LM, Foth BJ, McFadden GI, Muller S: The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases. Mol Microbiol. 2005 Jan;55(1):27-38.15612914Li XJ, Grunwald D, Mathieu J, Morel F, Stasia MJ: Crucial role of two potential cytosolic regions of Nox2, 191TSSTKTIRRS200 and 484DESQANHFAVHHDEEKD500, on NADPH oxidase activation. J Biol Chem. 2005 Apr 15;280(15):14962-73. Epub 2005 Jan 31.15684431Deres P, Halmosi R, Toth A, Kovacs K, Palfi A, Habon T, Czopf L, Kalai T, Hideg K, Sumegi B, Toth K: Prevention of doxorubicin-induced acute cardiotoxicity by an experimental antioxidant compound. J Cardiovasc Pharmacol. 2005 Jan;45(1):36-43.15613977Weitzman, P. D. J.; Hewson, Janet K.; Parker, M. G. Preparation of dihydrolipoamide by electrolytic reduction. FEBS Letters (1974), 43(1), 101-3.Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexP06959ODP2_ECOLIaceFhttp://ecmdb.ca/proteins/P06959.xmlDihydrolipoyl dehydrogenaseP0A9P0DLDH_ECOLIlpdAhttp://ecmdb.ca/proteins/P0A9P0.xmlDihydrolipoamide + NAD <> Lipoamide + NADH + Hydrogen ionR01698Acetyl-CoA + Dihydrolipoamide Coenzyme A + S-AcetyldihydrolipoamideDIHYDLIPACETRANS-RXNAcetyl-CoA + Dihydrolipoamide + Dihydrolipoamide <> Coenzyme A + S-AcetyldihydrolipoamidePW_R005172Succinyl-CoA + Dihydrolipoamide + Succinyl-CoA + Dihydrolipoamide > Coenzyme A + (S)-SuccinyldihydrolipoamidePW_R005173