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Gene Review

lpd  -  dihydrolipoyl dehydrogenase; E3 component...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0115, JW0112, dhl, lpdA
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Disease relevance of lpd


High impact information on lpd

  • In the absence of FAD, the dihydrolipoamide dehydrogenase monomer forms a stable folding intermediate, which is incapable of dimerization [6].
  • Wild-type dihydrolipoamide dehydrogenase is inactive with NADP, but the mutant enzyme displayed high levels of activity with this coenzyme, the values of Km, kcat, and kcat/Km comparing favorably with those found for the wild-type enzyme operating with NAD [7].
  • The expressed polypeptide consists of the lipoyl domain, inter-domain linker and peripheral subunit-binding domain; these were found to have folded into their native functional conformations as judged by reductive acetylation of the lipoyl domain, limited proteolysis of the linker region and ability to bind the dihydrolipoamide dehydrogenase dimer [8].
  • Residue 291 is near the middle of a long segment (about 30 amino acid residues) of polypeptide chain, rich in alanine, proline, and charged amino acids, that links the remaining lipoyl domain to the dihydrolipoamide dehydrogenase (E3) binding domain in the E2p chain [9].
  • This was tentatively attributed to another, but smaller, (alanine + proline)-rich sequence that separates the dihydrolipoamide dehydrogenase-binding domain from the inner core domain in the C-terminal half of the E2p chain [10].

Chemical compound and disease context of lpd


Biological context of lpd

  • The amino acid sequence of the peptide is identical to that of the inter-domain region (PEP3) linking the innermost of the three lipoyl domains to the dihydrolipoamide dehydrogenase-binding domain in the dihydrolipoamide acetyltransferase chain of the pyruvate dehydrogenase complex of Escherichia coli [13].
  • However, the selected transformants appeared to be heteroallelic, containing both the intact lpdA gene and the lpdA gene inactivated by the drug-resistance cassette [11].
  • The lpdA knockout mutant produced significantly more pyruvate and L-glutamate under aerobiosis [14].
  • In the present study, cell growth characteristics, enzyme activities and intracellular metabolite concentrations were compared between the parent strain Escherichia coli BW25113 and its lpdA knockout mutant in batch and continuous cultures [14].
  • The three homogeneous electron-transferring flavoproteins were very similar in their structural and biochemical properties to the dihydrolipoamide dehydrogenase of E. acidaminophilum and exhibited cross-reaction with antibodies raised against the latter enzyme [15].

Anatomical context of lpd

  • Citrate synthase was soluble and inactive, whereas dihydrolipoamide dehydrogenase was expressed as inclusion bodies [16].
  • In the present paper, a complete subcellular fractionation of T. brucei has been carried out and, by comparison with marker enzymes, it is confirmed that the dihydrolipoamide dehydrogenase is indeed associated with the plasma membrane [17].
  • Antigens of isolated bovine heart mitochondria reacting with antibodies of myocarditis serum on two-dimensional Western blots were identified by MALDI-TOF and NanoESI mass spectrometry as myosin heavy chain beta and as dihydrolipoamide dehydrogenase of the mitochondrial 2-oxoacid dehydrogenase complexes [18].

Associations of lpd with chemical compounds

  • The gene encoding the lipoamide dehydrogenase component of both the 2-oxoglutarate and pyruvate dehydrogenase complexes (E3; lpdA) is the distal gene of another cluster containing two promoters located at 2.7 min: Ppdh pdhR-aceEF-Plpd lpdA [19].
  • Reassociation to a fully active complex molecule works with equal facility between the pyruvate dehydrogenase component and a dihydrolipoamide transacetylase: dihydrolipoamide dehydrogenase subcomplex from either organism in all possible combinations [20].
  • The lpdA gene codes for a protein starting with methionine, which is post-translationally removed [11].
  • Flux analysis of the lpdA mutant indicated that the Entner-Doudoroff (ED) pathway and the glyoxylate shunt were activated [14].
  • The effect of the lpdA gene knockout on the intracellular metabolic flux distributions was investigated based on 1H-13C NMR spectra and GC-MS signals obtained from 13C-labeling experiment using the mixture of [U-13C] glucose, [1-13C] glucose, and naturally labeled glucose [14].

Other interactions of lpd

  • The responses of the suc and lpd promoters to different environmental conditions and to regulator defects were investigated with appropriate lacZ fusions, in order to understand how expression of the sucAB genes is co-regulated with other genes in the sdhCDAB-sucABCD cluster and with lpdA expression [19].
  • Thioredoxin elicits a new dihydrolipoamide dehydrogenase activity by interaction with the electron-transferring flavoprotein in Clostridium litoralis and Eubacterium acidaminophilum [21].

Analytical, diagnostic and therapeutic context of lpd


  1. Overproduction of the pyruvate dehydrogenase multienzyme complex of Escherichia coli and site-directed substitutions in the E1p and E2p subunits. Russell, G.C., Machado, R.S., Guest, J.R. Biochem. J. (1992) [Pubmed]
  2. Amino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex from Bacillus stearothermophilus. Packman, L.C., Borges, A., Perham, R.N. Biochem. J. (1988) [Pubmed]
  3. Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system. Krüger, N., Oppermann, F.B., Lorenzl, H., Steinbüchel, A. J. Bacteriol. (1994) [Pubmed]
  4. Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamide dehydrogenase. Hein, S., Steinbüchel, A. J. Bacteriol. (1994) [Pubmed]
  5. Mycobacterium tuberculosis lipoamide dehydrogenase is encoded by Rv0462 and not by the lpdA or lpdB genes. Argyrou, A., Blanchard, J.S. Biochemistry (2001) [Pubmed]
  6. FAD insertion is essential for attaining the assembly competence of the dihydrolipoamide dehydrogenase (E3) monomer from Escherichia coli. Lindsay, H., Beaumont, E., Richards, S.D., Kelly, S.M., Sanderson, S.J., Price, N.C., Lindsay, J.G. J. Biol. Chem. (2000) [Pubmed]
  7. Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering. Bocanegra, J.A., Scrutton, N.S., Perham, R.N. Biochemistry (1993) [Pubmed]
  8. Expression in Escherichia coli of a sub-gene encoding the lipoyl and peripheral subunit-binding domains of the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex of Bacillus stearothermophilus. Hipps, D.S., Perham, R.N. Biochem. J. (1992) [Pubmed]
  9. Site-directed mutagenesis and 1H NMR spectroscopy of an interdomain segment in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Texter, F.L., Radford, S.E., Laue, E.D., Perham, R.N., Miles, J.S., Guest, J.R. Biochemistry (1988) [Pubmed]
  10. Segmental structure and protein domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Genetic reconstruction in vitro and 1H-n.m.r. spectroscopy. Radford, S.E., Laue, E.D., Perham, R.N., Miles, J.S., Guest, J.R. Biochem. J. (1987) [Pubmed]
  11. Characterization of a gene encoding dihydrolipoamide dehydrogenase of the cyanobacterium Synechocystis sp. strain PCC 6803. Engels, A., Pistorius, E.K. Microbiology (Reading, Engl.) (1997) [Pubmed]
  12. Co-regulation of lipoamide dehydrogenase and 2-oxoglutarate dehydrogenase synthesis in Escherichia coli: characterisation of an ArcA binding site in the lpd promoter. Cunningham, L., Georgellis, D., Green, J., Guest, J.R. FEMS Microbiol. Lett. (1998) [Pubmed]
  13. Antibodies against an inter-domain segment of polypeptide chain inhibit active-site coupling in the pyruvate dehydrogenase multienzyme complex. Radford, S.E., Perham, R.N., Ullrich, S.J., Appella, E. FEBS Lett. (1989) [Pubmed]
  14. Effect of lpdA gene knockout on the metabolism in Escherichia coli based on enzyme activities, intracellular metabolite concentrations and metabolic flux analysis by 13C-labeling experiments. Li, M., Ho, P.Y., Yao, S., Shimizu, K. J. Biotechnol. (2006) [Pubmed]
  15. Purification of NADPH-dependent electron-transferring flavoproteins and N-terminal protein sequence data of dihydrolipoamide dehydrogenases from anaerobic, glycine-utilizing bacteria. Dietrichs, D., Meyer, M., Schmidt, B., Andreesen, J.R. J. Bacteriol. (1990) [Pubmed]
  16. Expression, reactivation, and purification of enzymes from Haloferax volcanii in Escherichia coli. Connaris, H., Chaudhuri, J.B., Danson, M.J., Hough, D.W. Biotechnol. Bioeng. (1999) [Pubmed]
  17. Subcellular localisation of dihydrolipoamide dehydrogenase and detection of lipoic acid in bloodstream forms of Trypanosoma brucei. Jackman, S.A., Hough, D.W., Danson, M.J., Stevenson, K.J., Opperdoes, F.R. Eur. J. Biochem. (1990) [Pubmed]
  18. 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]
  19. Transcription and transcript processing in the sdhCDAB-sucABCD operon of Escherichia coli. Cunningham, L., Guest, J.R. Microbiology (Reading, Engl.) (1998) [Pubmed]
  20. Purification and properties of the pyruvate dehydrogenase complex from Salmonella typhimurium and formation of hybrids with the enzyme complex from Escherichia coli. Seckler, R., Binder, R., Bisswanger, H. Biochim. Biophys. Acta (1982) [Pubmed]
  21. Thioredoxin elicits a new dihydrolipoamide dehydrogenase activity by interaction with the electron-transferring flavoprotein in Clostridium litoralis and Eubacterium acidaminophilum. Meyer, M., Dietrichs, D., Schmidt, B., Andreesen, J.R. J. Bacteriol. (1991) [Pubmed]
  22. The steady-state internal redox state (NADH/NAD) reflects the external redox state and is correlated with catabolic adaptation in Escherichia coli. de Graef, M.R., Alexeeva, S., Snoep, J.L., Teixeira de Mattos, M.J. J. Bacteriol. (1999) [Pubmed]
  23. Expression in Escherichia coli of the lpdA gene, protein sequence analysis and immunological characterization of the P64k protein from Neisseria meningitidis. Guillén, G., Alvarez, A., Silva, R., Morera, V., González, S., Musacchio, A., Besada, V., Coizeau, E., Caballero, E., Nazabal, C., Carmenate, T., González, L.J., Estrada, R., Támbara, Y., Padrón, G., Herrera, L. Biotechnol. Appl. Biochem. (1998) [Pubmed]
  24. Cloning, sequencing, and expression of Trypanosoma brucei dihydrolipoamide dehydrogenase. Else, A.J., Hough, D.W., Danson, M.J. Eur. J. Biochem. (1993) [Pubmed]
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