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Gene Review

DLD  -  dihydrolipoamide dehydrogenase

Sus scrofa

 
 
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Disease relevance of DLD

 

High impact information on DLD

 

Chemical compound and disease context of DLD

 

Biological context of DLD

 

Anatomical context of DLD

 

Associations of DLD with chemical compounds

 

Other interactions of DLD

 

Analytical, diagnostic and therapeutic context of DLD

References

  1. Lipoamide dehydrogenase from Escherichia coli. Steady-state kinetics of the physiological reaction. Sahlman, L., Williams, C.H. J. Biol. Chem. (1989) [Pubmed]
  2. pH-dependent substrate preference of pig heart lipoamide dehydrogenase varies with oligomeric state: response to mitochondrial matrix acidification. Klyachko, N.L., Shchedrina, V.A., Efimov, A.V., Kazakov, S.V., Gazaryan, I.G., Kristal, B.S., Brown, A.M. J. Biol. Chem. (2005) [Pubmed]
  3. Deficiency of pyruvate dehydrogenase complex (PDHC) in Leigh's disease fibroblasts: an abnormality in lipoamide dehydrogenase affecting PDHC activation. Hinman, L.M., Sheu, K.F., Baker, A.C., Kim, Y.T., Blass, J.P. Neurology (1989) [Pubmed]
  4. Purification and characterization of lipoamide dehydrogenase from Trypanosoma cruzi. Lohrer, H., Krauth-Siegel, R.L. Eur. J. Biochem. (1990) [Pubmed]
  5. Cloning, sequence and transcriptional analysis of the structural gene for LPD-3, the third lipoamide dehydrogenase of Pseudomonas putida. Palmer, J.A., Madhusudhan, K.T., Hatter, K., Sokatch, J.R. Eur. J. Biochem. (1991) [Pubmed]
  6. Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase. Williams, C.H., Arscott, L.D., Schulz, G.E. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  7. Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase. Gazaryan, I.G., Krasnikov, B.F., Ashby, G.A., Thorneley, R.N., Kristal, B.S., Brown, A.M. J. Biol. Chem. (2002) [Pubmed]
  8. The sequence of amino acid residues around the oxidation-reduction active disulfide in yeast glutathione reductase. Jones, E.T., Williams, C.H. J. Biol. Chem. (1975) [Pubmed]
  9. The amino acid sequence encompassing the active-site histidine residue of lipoamide dehydrogenase from Escherichia coli labelled with a bifunctional arsenoxide. Holmes, C.F., Stevenson, K.J. Biochem. Cell Biol. (1986) [Pubmed]
  10. Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases. Otulakowski, G., Robinson, B.H. J. Biol. Chem. (1987) [Pubmed]
  11. Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase. Thorpe, C., Williams, C.H. J. Biol. Chem. (1976) [Pubmed]
  12. Immunological and biosynthetic studies on the mammalian 2-oxoglutarate dehydrogenase multienzyme complex. Hunter, A., Lindsay, J.G. Eur. J. Biochem. (1986) [Pubmed]
  13. The ratio of 3-hydroxyacyl-CoA dehydrogenase to lipoamide dehydrogenase activity in individual muscle fibers: mitochondrial specialization for source of energy. Hirsch, H.E., Parks, M.E., Blanco, C.E., Simpson, D.R. J. Neurosci. Res. (1982) [Pubmed]
  14. Spectral evidence for a flavin adduct in a monoalkylated derivative of pig heart lipoamide dehydrogenase. Thorpe, C., Williams, C.H. J. Biol. Chem. (1976) [Pubmed]
  15. Reactions of pig heart lipoamide dehydrogenase with pyridine nucleotides. Evidence for an effector role for bound oxidized pyridine nucleotide. Matthews, R.G., Ballou, D.P., Williams, C.H. J. Biol. Chem. (1979) [Pubmed]
  16. Ion pair formation in pig heart lipoamide dehydrogenase: rationalization of pH profiles for reactivity of oxidized enzyme with dihydrolipoamide and 2-electron-reduced enzyme with lipoamide and iodoacetamide. Matthews, R.G., Ballou, D.P., Thorpe, C., Williams, C.H. J. Biol. Chem. (1977) [Pubmed]
  17. Antibodies to bovine liver branched-chain 2-oxo acid dehydrogenase cross-react with this enzyme complex from other tissues and species. Heffelfinger, S.C., Sewell, E.T., Danner, D.J. Biochem. J. (1983) [Pubmed]
  18. The mechanism of the quinone reductase reaction of pig heart lipoamide dehydrogenase. Vienozinskis, J., Butkus, A., Cenas, N., Kulys, J. Biochem. J. (1990) [Pubmed]
  19. Biosynthesis, import and processing of precursor polypeptides of mammalian mitochondrial pyruvate dehydrogenase complex. De Marcucci, O.G., Gibb, G.M., Dick, J., Lindsay, J.G. Biochem. J. (1988) [Pubmed]
  20. Superoxide anion production by lipoamide dehydrogenase redox-cycling: effect of enzyme modifiers. Grinblat, L., Sreider, C.M., Stoppani, A.O. Biochem. Int. (1991) [Pubmed]
  21. Sulfoxide reduction catalyzed by guinea pig liver aldehyde oxidase in combination with one-electron reducing flavoenzymes. Yoshihara, S., Tatsumi, K. J. Pharmacobio-dyn. (1985) [Pubmed]
  22. Titration studies on the active sites of pig heart lipoamide dehydrogenase and yeast glutathione reductase as monitored by the charge transfer absorbance. Sahlman, L., Williams, C.H. J. Biol. Chem. (1989) [Pubmed]
  23. Magnetic circular dichroism studies on the active-site flavin of lipoamide dehydrogenase. Templeton, D.M., Hollebone, B.R., Tsai, C.S. Biochemistry (1980) [Pubmed]
  24. A pulse fluorometry study of lipoamide dehydrogenase. Evidence for non-equivalent FAD centers. Wahl, P., Auchet, J.C., Visser, A.J., Veeger, C. Eur. J. Biochem. (1975) [Pubmed]
  25. Crystallization and preliminary X-ray analysis of pig E3, lipoamide dehydrogenase. Toyoda, T., Kobayashi, R., Sekiguchi, T., Koike, K., Koike, M., Takenaka, A. Acta Crystallogr. D Biol. Crystallogr. (1998) [Pubmed]
 
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