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Chemical Compound Review

AG-F-37054     6,8-bis-sulfanyloctanamide

Synonyms: CHEBI:17694, HMDB00985, CTK4I0567, AC1L19QN, C00579, ...
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Disease relevance of Dihydrothioctamide


Psychiatry related information on Dihydrothioctamide


High impact information on Dihydrothioctamide


Chemical compound and disease context of Dihydrothioctamide


Biological context of Dihydrothioctamide


Anatomical context of Dihydrothioctamide


Associations of Dihydrothioctamide with other chemical compounds


Gene context of Dihydrothioctamide

  • Mutations in DLAT, the gene encoding dihydrolipoamide acetyltransferase, the E2 core component of the complex, have not been described previously [29].
  • The maximum activation by dihydrolipoamide acetyltransferase was demonstrated by PDK3 [30].
  • The activity of the four PDKs was stimulated to a different extent by the reduction and acetylation state of the lipoyl moieties of dihydrolipoamide acetyltransferase with the maximum stimulation of PDK2 [30].
  • The Brucella melitensis sucB gene encoding the dihydrolipoamide succinyltransferase (E2o) enzyme (previously identified as an immunogenic protein in infected sheep) was cloned and sequenced [31].
  • Since lipoic acids inhibited PDKs activity both when reconstituted in PDC and in the presence of E1 alone, dissociation of PDK from the lipoyl domains of dihydrolipoamide acetyltransferase in the presence of lipoic acids is not a likely explanation for inhibition [32].

Analytical, diagnostic and therapeutic context of Dihydrothioctamide


  1. The autoepitope of the 74-kD mitochondrial autoantigen of primary biliary cirrhosis corresponds to the functional site of dihydrolipoamide acetyltransferase. Van de Water, J., Gershwin, M.E., Leung, P., Ansari, A., Coppel, R.L. J. Exp. Med. (1988) [Pubmed]
  2. Nucleotide sequence for yeast dihydrolipoamide dehydrogenase. Browning, K.S., Uhlinger, D.J., Reed, L.J. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  3. Immunization of experimental animals with dihydrolipoamide acetyltransferase, as a purified recombinant polypeptide, generates mitochondrial antibodies but not primary biliary cirrhosis. Krams, S.M., Surh, C.D., Coppel, R.L., Ansari, A., Ruebner, B., Gershwin, M.E. Hepatology (1989) [Pubmed]
  4. Autoantibodies of primary biliary cirrhosis recognize dihydrolipoamide acetyltransferase and inhibit enzyme function. Van de Water, J., Fregeau, D., Davis, P., Ansari, A., Danner, D., Leung, P., Coppel, R., Gershwin, M.E. J. Immunol. (1988) [Pubmed]
  5. The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Kalia, Y.N., Brocklehurst, S.M., Hipps, D.S., Appella, E., Sakaguchi, K., Perham, R.N. J. Mol. Biol. (1993) [Pubmed]
  6. Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex. Nakano, K., Takase, C., Sakamoto, T., Nakagawa, S., Inazawa, J., Ohta, S., Matuda, S. Eur. J. Biochem. (1994) [Pubmed]
  7. The human biliary epithelial cell plasma membrane antigen in primary biliary cirrhosis: pyruvate dehydrogenase X? Joplin, R.E., Wallace, L.L., Lindsay, J.G., Palmer, J.M., Yeaman, S.J., Neuberger, J.M. Gastroenterology (1997) [Pubmed]
  8. Membrane dihydrolipoamide acetyltransferase (E2) on human biliary epithelial cells in primary biliary cirrhosis. Joplin, R., Lindsay, J.G., Johnson, G.D., Strain, A., Neuberger, J. Lancet (1992) [Pubmed]
  9. Conservation of synteny between the genome of the pufferfish (Fugu rubripes) and the region on human chromosome 14 (14q24.3) associated with familial Alzheimer disease (AD3 locus). Trower, M.K., Orton, S.M., Purvis, I.J., Sanseau, P., Riley, J., Christodoulou, C., Burt, D., See, C.G., Elgar, G., Sherrington, R., Rogaev, E.I., St George-Hyslop, P., Brenner, S., Dykes, C.W. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  10. A lipoyl synthetic octadecapeptide of dihydrolipoamide acetyltransferase specifically recognized by anti-M2 autoantibodies in primary biliary cirrhosis. Tuaillon, N., Andre, C., Briand, J.P., Penner, E., Muller, S. J. Immunol. (1992) [Pubmed]
  11. Purification and comparative studies of dihydrolipoamide dehydrogenases from the anaerobic, glycine-utilizing bacteria Peptostreptococcus glycinophilus, Clostridium cylindrosporum, and Clostridium sporogenes. Dietrichs, D., Andreesen, J.R. J. Bacteriol. (1990) [Pubmed]
  12. Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase. Spencer, M.E., Darlison, M.G., Stephens, P.E., Duckenfield, I.K., Guest, J.R. Eur. J. Biochem. (1984) [Pubmed]
  13. Rhodanese from Thiobacillus A2: determination of activity by proton nuclear magnetic resonance spectroscopy. Silver, M., Howarth, O.W., Kelly, D.P. J. Gen. Microbiol. (1976) [Pubmed]
  14. Rhodanese from Thiobacillus A2: catalysis of reactions of thiosulphate with dihydrolipoate and dihydrolipoamide. Silver, M., Kelly, D.P. J. Gen. Microbiol. (1976) [Pubmed]
  15. Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae. Behal, R.H., Browning, K.S., Hall, T.B., Reed, L.J. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  16. A zebrafish model for pyruvate dehydrogenase deficiency: rescue of neurological dysfunction and embryonic lethality using a ketogenic diet. Taylor, M.R., Hurley, J.B., Van Epps, H.A., Brockerhoff, S.E. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  17. Functional analysis in Saccharomyces cerevisiae of naturally occurring amino acid substitutions in human dihydrolipoamide dehydrogenase. Lanterman, M.M., Dickinson, J.R., Danner, D.J. Hum. Mol. Genet. (1996) [Pubmed]
  18. Association between the gene encoding the E2 subunit of the alpha-ketoglutarate dehydrogenase complex and Parkinson's disease. Kobayashi, T., Matsumine, H., Matuda, S., Mizuno, Y. Ann. Neurol. (1998) [Pubmed]
  19. The relative affinity of recombinant dihydrolipoamide transacetylase for autoantibodies in primary biliary cirrhosis. Robertson, C.A., Coppel, R.L., Prindiville, T., Fregeau, D., Kaplan, M., Dickson, E.R., Gershwin, M.E. Hepatology (1990) [Pubmed]
  20. Distribution of dihydrolipoamide acetyltransferase (E2) in the liver and portal lymph nodes of patients with primary biliary cirrhosis: an immunohistochemical study. Joplin, R., Lindsay, J.G., Hubscher, S.G., Johnson, G.D., Shaw, J.C., Strain, A.J., Neuberger, J.M. Hepatology (1991) [Pubmed]
  21. Enhanced ADP-ribosylation and its diminution by lipoamide after ischemia-reperfusion in perfused rat heart. Szabados, E., Fischer, G.M., Gallyas, F., Kispal, G., Sumegi, B. Free Radic. Biol. Med. (1999) [Pubmed]
  22. Novel tyrosine-phosphorylated post-pyruvate metabolic enzyme, dihydrolipoamide dehydrogenase, involved in capacitation of hamster spermatozoa. Mitra, K., Shivaji, S. Biol. Reprod. (2004) [Pubmed]
  23. Specific reduction of insulin disulfides by macrophage migration inhibitory factor (MIF) with glutathione and dihydrolipoamide: potential role in cellular redox processes. Kleemann, R., Mischke, R., Kapurniotu, A., Brunner, H., Bernhagen, J. FEBS Lett. (1998) [Pubmed]
  24. A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane in skeletal muscle. Matuda, S., Kodama, J., Goshi, N., Takase, C., Nakano, K., Nakagawa, S., Ohta, S. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  25. Distribution of pyruvate dehydrogenase dihydrolipoamide acetyltransferase (PDC-E2) and another mitochondrial marker in salivary gland and biliary epithelium from patients with primary biliary cirrhosis. Joplin, R.E., Johnson, G.D., Matthews, J.B., Hamburger, J., Lindsay, J.G., Hubscher, S.G., Strain, A.J., Neuberger, J.M. Hepatology (1994) [Pubmed]
  26. Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart. Matthews, R.G., Williams, C.H. J. Biol. Chem. (1976) [Pubmed]
  27. 13C nuclear magnetic resonance study of the pyruvate dehydrogenase-catalyzed acetylation of dihydrolipoamide. O'Connor, T.P., Roche, T.E., Paukstelis, J.V. J. Biol. Chem. (1982) [Pubmed]
  28. Molecular characterization of the trypanothione reductase gene from Crithidia fasciculata and Trypanosoma brucei: comparison with other flavoprotein disulphide oxidoreductases with respect to substrate specificity and catalytic mechanism. Aboagye-Kwarteng, T., Smith, K., Fairlamb, A.H. Mol. Microbiol. (1992) [Pubmed]
  29. Clinical and genetic spectrum of pyruvate dehydrogenase deficiency: dihydrolipoamide acetyltransferase (E2) deficiency. Head, R.A., Brown, R.M., Zolkipli, Z., Shahdadpuri, R., King, M.D., Clayton, P.T., Brown, G.K. Ann. Neurol. (2005) [Pubmed]
  30. Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase. Korotchkina, L.G., Patel, M.S. J. Biol. Chem. (2001) [Pubmed]
  31. Cloning, nucleotide sequence, and expression of the Brucella melitensis sucB gene coding for an immunogenic dihydrolipoamide succinyltransferase homologous protein. Zygmunt, M.S., Díaz, M.A., Teixeira-Gomes, A.P., Cloeckaert, A. Infect. Immun. (2001) [Pubmed]
  32. R-lipoic acid inhibits mammalian pyruvate dehydrogenase kinase. Korotchkina, L.G., Sidhu, S., Patel, M.S. Free Radic. Res. (2004) [Pubmed]
  33. Three-dimensional structure of the truncated core of the Saccharomyces cerevisiae pyruvate dehydrogenase complex determined from negative stain and cryoelectron microscopy images. Stoops, J.K., Baker, T.S., Schroeter, J.P., Kolodziej, S.J., Niu, X.D., Reed, L.J. J. Biol. Chem. (1992) [Pubmed]
  34. Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The "breathing" core and its functional relationship to protein dynamics. Zhou, Z.H., Liao, W., Cheng, R.H., Lawson, J.E., McCarthy, D.B., Reed, L.J., Stoops, J.K. J. Biol. Chem. (2001) [Pubmed]
  35. Immunochemical identification of coenzyme Q0-dihydrolipoamide adducts in the E2 components of the alpha-ketoglutarate and pyruvate dehydrogenase complexes partially explains the cellular toxicity of coenzyme Q0. MacDonald, M.J., Husain, R.D., Hoffmann-Benning, S., Baker, T.R. J. Biol. Chem. (2004) [Pubmed]
  36. The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases. McMillan, P.J., Stimmler, L.M., Foth, B.J., McFadden, G.I., Müller, S. Mol. Microbiol. (2005) [Pubmed]
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