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Gene Review

lpdA  -  dihydrolipoamide dehydrogenase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of lpdA


High impact information on lpdA

  • Based on the fluorescence lifetime distributions, the mutants Y177F and Y177G have a more flexible protein structure than wild-type GR: in the range of 223 K to 277 K in 80% glycerol, both tyrosine mutants mimic the closely related enzyme dihydrolipoyl dehydrogenase [5].
  • Primary structures derived from human and bovine E2 cDNAs show leader sequences including the initiator methionine and the homologous mature peptides consisting of complete lipoyl-bearing and dihydrolipoyl dehydrogenase (E3) binding domains and two hinge regions [6].
  • The time-resolved anisotropy of FAD in the native complex and in the isolated dihydrolipoyl dehydrogenase indicates some rapid local mobility of the FAD (rotational correlation time of 12 ns) that is viscosity independent, as well as a component of the anisotropy that is constant over the 35-ns time scale of the experiments [7].
  • Fluorescence energy transfer measurements between bound epsilonCoA on the dihydrolipoyl transacetylase enzyme and flavin adenine dinucleotide on the dihydrolipoyl dehydrogenase enzyme either in the complex or subcomplex indicate, assuming the emission and absorption dipoles are randomly oriented, that these two probes must be at least 50 A apart [8].
  • These results indicated the involvement of the third complex component, dihydrolipoyl dehydrogenase, in the 2-oxoacid-dependent dihydrolipoate formation [9].

Biological context of lpdA

  • The amino-acid sequence of the N-terminal region is homologous with the lipoyl domains of the dihydrolipoyl acyltransferase (E2) components, and that of the C-terminal region with the dihydrolipoyl dehydrogenase (E3) components, of 2-oxo acid dehydrogenase multienzyme complexes [3].

Anatomical context of lpdA

  • These inclusion bodies additionally contain significant amounts of the heat-shock chaperone DnaK, and putative DnaK substrates such as the elongation factor Tu (ET-Tu) and the metabolic enzymes dihydrolipoamide dehydrogenase (LpdA), tryptophanase (TnaA), and d-tagatose-1,6-bisphosphate aldolase (GatY) [10].

Associations of lpdA with chemical compounds

  • On Western blots, antibodies raised against dihydrolipoamide dehydrogenase from the stereorarian trypanosome, Trypanosoma cruzi, cross-react strongly with the dihydrolipoamide dehydrogenase from all three T. brucei species; by this method, the relative molecular masses of their dihydrolipoamide dehydrogenases are indistinguishable [11].

Physical interactions of lpdA


Analytical, diagnostic and therapeutic context of lpdA

  • Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs [6].


  1. Mycobacterium tuberculosis lipoamide dehydrogenase is encoded by Rv0462 and not by the lpdA or lpdB genes. Argyrou, A., Blanchard, J.S. Biochemistry (2001) [Pubmed]
  2. Configuration of interdomain linkers in pyruvate dehydrogenase complex of Escherichia coli as determined by cryoelectron microscopy. Wagenknecht, T., Grassucci, R., Berkowitz, J., Forneris, C. J. Struct. Biol. (1992) [Pubmed]
  3. Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis. Tozawa, K., Broadhurst, R.W., Raine, A.R., Fuller, C., Alvarez, A., Guillen, G., Padron, G., Perham, R.N. Eur. J. Biochem. (2001) [Pubmed]
  4. Analysis of mitochondrial antigens reveals inner membrane succinate dehydrogenase flavoprotein subunit as autoantigen to antibodies in anti-M7 sera. Cicek, G., Schiltz, E., Hess, D., Staiger, J., Brandsch, R. Clin. Exp. Immunol. (2002) [Pubmed]
  5. Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase. van den Berg, P.A., van Hoek, A., Walentas, C.D., Perham, R.N., Visser, A.J. Biophys. J. (1998) [Pubmed]
  6. Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. Lau, K.S., Griffin, T.A., Hu, C.W., Chuang, D.T. Biochemistry (1988) [Pubmed]
  7. Fluorescence polarization study of the alpha-ketoglutarate dehydrogenase complex from Escherichia coli. Waskiewicz, D.E., Hammes, G.G. Biochemistry (1982) [Pubmed]
  8. Fluorescence energy-transfer measurements between coenzyme A and flavin adenine dinucleotide binding sites of the Escherichia coli pyruvate dehydrogenase multienzyme complex. Shepherd, G.B., Papadakis, N. Biochemistry (1976) [Pubmed]
  9. Using lipoate enantiomers and thioredoxin to study the mechanism of the 2-oxoacid-dependent dihydrolipoate production by the 2-oxoacid dehydrogenase complexes. Bunik, V., Shoubnikova, A., Loeffelhardt, S., Bisswanger, H., Borbe, H.O., Follmann, H. FEBS Lett. (1995) [Pubmed]
  10. Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli. Rinas, U., Hoffmann, F., Betiku, E., Estap??, D., Marten, S. J. Biotechnol. (2007) [Pubmed]
  11. Dihydrolipoamide dehydrogenase in the trypanosoma subgenus, trypanozoon. Else, A.J., Clarke, J.F., Willis, A., Jackman, S.A., Hough, D.W., Danson, M.J. Mol. Biochem. Parasitol. (1994) [Pubmed]
  12. Role of excess lipoyl dehydrogenase in reconstituted alpha-ketoglutarate dehydrogenase complex of Escherichia coli. Wagenknecht, T., Francis, N., DeRosier, D. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
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