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Chemical Compound Review

CHEBI:43711     (6R)-6,8-bis- sulfanyloctanamide

Synonyms: AC1L9HIU, C8H17NOS2, DB08120, LPM, (R)-dihydrolipoamide, ...
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Disease relevance of lipoamide

  • In conclusion, three lines of evidence indicate that the mechanism of human thioredoxin reductase is like the mechanisms of lipoamide dehydrogenase and glutathione reductase and differs fundamentally from the mechanism of E. coli thioredoxin reductase [1].
  • Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis [2].
  • The structure of lipoamide dehydrogenase from Azotobacter vinelandii has been refined by the molecular dynamics technique to an R-factor of 19.8% at 2.2 A resolution [3].
  • The structure of Pseudomonas fluorescens lipoamide dehydrogenase, a dimeric flavoenzyme with a molecular mass of 106,000 daltons, was solved by the molecular replacement method and refined to an R-factor of 19.4% at 2.8 A resolution [4].
  • Preclinical diagnosis and carrier detection in ataxia associated with abnormalities of lipoamide dehydrogenase [5].

High impact information on lipoamide


Chemical compound and disease context of lipoamide


Biological context of lipoamide


Anatomical context of lipoamide


Associations of lipoamide with other chemical compounds


Gene context of lipoamide

  • 2-Oxoglutarate dehydrogenase (lipoamide) (( OGDH: 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating), EC )) is a component enzyme of the 2-oxoglutarate dehydrogenase complex [16].
  • In addition we also report the in vivo modification of lipoamide present in the above-mentioned E2 subunits under the stressing conditions tested and that this also occurs with the homologous enzymes present in Escherichia coli cells that were used for comparative analysis [28].
  • Transcription factor GCN4 for control of amino acid biosynthesis also regulates the expression of the gene for lipoamide dehydrogenase [29].
  • Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase [30].
  • A sample of colonies from the Clarke-Carbon ColE1-Escherichia coli DNA plasmid gene bank was screened by conjugation for complementation of the lipoamide dehydrogenase lesion of a deletion strain lacking all components of the pyruvate dehydrogenase complex, delta (aroP aceE aceF lpd) [31].

Analytical, diagnostic and therapeutic context of lipoamide


  1. The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli. Arscott, L.D., Gromer, S., Schirmer, R.H., Becker, K., Williams, C.H. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  2. Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis. Rajashankar, K.R., Bryk, R., Kniewel, R., Buglino, J.A., Nathan, C.F., Lima, C.D. J. Biol. Chem. (2005) [Pubmed]
  3. Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase. Mattevi, A., Schierbeek, A.J., Hol, W.G. J. Mol. Biol. (1991) [Pubmed]
  4. Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8 A resolution. Analysis of redox and thermostability properties. Mattevi, A., Obmolova, G., Kalk, K.H., van Berkel, W.J., Hol, W.G. J. Mol. Biol. (1993) [Pubmed]
  5. Preclinical diagnosis and carrier detection in ataxia associated with abnormalities of lipoamide dehydrogenase. Kark, R.A., Rodriguez-Budelli, M., Perlman, S., Gulley, W.F., Torok, K. Neurology (1980) [Pubmed]
  6. Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex. Mattevi, A., Obmolova, G., Schulze, E., Kalk, K.H., Westphal, A.H., de Kok, A., Hol, W.G. Science (1992) [Pubmed]
  7. Deficiency of the pyruvate dehydrogenase component in pyruvate dehydrogenase complex-deficient human fibroblasts. Immunological identification. Ho, L., Hu, C.W., Packman, S., Patel, M.S. J. Clin. Invest. (1986) [Pubmed]
  8. Defective glycine cleavage system in nonketotic hyperglycinemia. Occurrence of a less active glycine decarboxylase and an abnormal aminomethyl carrier protein. Hiraga, K., Kochi, H., Hayasaka, K., Kikuchi, G., Nyhan, W.L. J. Clin. Invest. (1981) [Pubmed]
  9. S-nitroso proteome of Mycobacterium tuberculosis: Enzymes of intermediary metabolism and antioxidant defense. Rhee, K.Y., Erdjument-Bromage, H., Tempst, P., Nathan, C.F. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  10. Mitochondrial stress protein recognition of inactivated dehydrogenases during mammalian cell death. Bruschi, S.A., Lindsay, J.G., Crabb, J.W. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  11. Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolase. Nemeria, N., Arjunan, P., Brunskill, A., Sheibani, F., Wei, W., Yan, Y., Zhang, S., Jordan, F., Furey, W. Biochemistry (2002) [Pubmed]
  12. Comparison of the dynamical structures of lipoamide dehydrogenase and glutathione reductase by time-resolved polarized flavin fluorescence. Bastiaens, P.I., van Hoek, A., Wolkers, W.F., Brochon, J.C., Visser, A.J. Biochemistry (1992) [Pubmed]
  13. Modulation of the oxidation-reduction potential of the flavin in lipoamide dehydrogenase from Escherichia coli by alteration of a nearby charged residue, K53R. Maeda-Yorita, K., Russell, G.C., Guest, J.R., Massey, V., Williams, C.H. Biochemistry (1994) [Pubmed]
  14. Inhibition of pyruvate dehydrogenase multienzyme complex from Escherichia coli with a radiolabeled bifunctional arsenoxide: evidence for an essential histidine residue at the active site of lipoamide dehydrogenase. Adamson, S.R., Robinson, J.A., Stevenson, K.J. Biochemistry (1984) [Pubmed]
  15. Inhibition of pyruvate dehydrogenase multienzyme complex from Escherichia coli with a bifunctional arsenoxide: selective inactivation of lipoamide dehydrogenase. Adamson, S.R., Stevenson, K.J. Biochemistry (1981) [Pubmed]
  16. Cloning and nucleotide sequence of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide). Koike, K., Urata, Y., Goto, S. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  17. Three genes for enzymes of the pyruvate dehydrogenase complex map to human chromosomes 3, 7, and X. Olson, S., Song, B.J., Huh, T.L., Chi, Y.T., Veech, R.L., McBride, O.W. Am. J. Hum. Genet. (1990) [Pubmed]
  18. Inherited depression of arterial lipoamide dehydrogenase activity associated with susceptibility to atherosclerosis in pigeons. Zemplenyi, T., Blankenhorn, D.H., Rosenstein, A.J. Circ. Res. (1975) [Pubmed]
  19. Yeast intragenic transcriptional control: activation and repression sites within the coding region of the Saccharomyces cerevisiae LPD1 gene. Sinclair, D.A., Kornfeld, G.D., Dawes, I.W. Mol. Cell. Biol. (1994) [Pubmed]
  20. Flavoprotein structure and mechanism. 5. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design. Krauth-Siegel, R.L., Schöneck, R. FASEB J. (1995) [Pubmed]
  21. Validation of lucigenin (bis-N-methylacridinium) as a chemilumigenic probe for detecting superoxide anion radical production by enzymatic and cellular systems. Li, Y., Zhu, H., Kuppusamy, P., Roubaud, V., Zweier, J.L., Trush, M.A. J. Biol. Chem. (1998) [Pubmed]
  22. Structural relationship between glutathione reductase and lipoamide dehydrogenase. Rice, D.W., Schulz, G.E., Guest, J.R. J. Mol. Biol. (1984) [Pubmed]
  23. 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]
  24. Regulation of cellular thiols in human lymphocytes by alpha-lipoic acid: a flow cytometric analysis. Sen, C.K., Roy, S., Han, D., Packer, L. Free Radic. Biol. Med. (1997) [Pubmed]
  25. Microsomal lipoamide reductase provides vitamin K epoxide reductase with reducing equivalents. Thijssen, H.H., Janssen, Y.P., Vervoort, L.T. Biochem. J. (1994) [Pubmed]
  26. Site-to-site directed immobilization of enzymes with bis-NAD analogues. Månsson, M.O., Siegbahn, N., Mosbach, K. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  27. Riboflavin uptake and FAD synthesis in Saccharomyces cerevisiae mitochondria: involvement of the Flx1p carrier in FAD export. Bafunno, V., Giancaspero, T.A., Brizio, C., Bufano, D., Passarella, S., Boles, E., Barile, M. J. Biol. Chem. (2004) [Pubmed]
  28. Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. Cabiscol, E., Piulats, E., Echave, P., Herrero, E., Ros, J. J. Biol. Chem. (2000) [Pubmed]
  29. Transcription factor GCN4 for control of amino acid biosynthesis also regulates the expression of the gene for lipoamide dehydrogenase. Zaman, Z., Bowman, S.B., Kornfeld, G.D., Brown, A.J., Dawes, I.W. Biochem. J. (1999) [Pubmed]
  30. Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase. Arnér, E.S., Nordberg, J., Holmgren, A. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  31. Hybrid plasmids containing the pyruvate dehydrogenase complex genes and gene-DNA relationships in the 2 to 3 minute region of the Escherichia coli chromosome. Guest, J.R., Roberts, R.E., Stephens, P.E. J. Gen. Microbiol. (1983) [Pubmed]
  32. Crystallization and preliminary X-ray investigation of lipoamide dehydrogenase from Azotobacter vinelandii. Schierbeek, A.J., van der Laan, J.M., Groendijk, H., Wierenga, R.K., Drenth, J. J. Mol. Biol. (1983) [Pubmed]
  33. Cytosolic cofactors and dihydrolipoamide stimulate hepatic microsomal 5'-deiodination. Sawada, K., Hummel, B.C., Walfish, P.G. Endocrinology (1985) [Pubmed]
  34. Low immunogenicity of the common lipoamide dehydrogenase subunit (E3) of mammalian pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multienzyme complexes. De Marcucci, O.L., Hunter, A., Lindsay, J.G. Biochem. J. (1985) [Pubmed]
  35. An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide. Miller, H., Mande, S.S., Parsonage, D., Sarfaty, S.H., Hol, W.G., Claiborne, A. Biochemistry (1995) [Pubmed]
  36. Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Spectral properties of wild type and mutated enzymes. Benen, J., van Berkel, W., Zak, Z., Visser, T., Veeger, C., de Kok, A. Eur. J. Biochem. (1991) [Pubmed]
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