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LPD1  -  dihydrolipoyl dehydrogenase

Saccharomyces cerevisiae S288c

Synonyms: DHLP1, Dihydrolipoamide dehydrogenase, Dihydrolipoyl dehydrogenase, mitochondrial, Glycine decarboxylase complex subunit L, Lipoamide dehydrogenase component of pyruvate dehydrogenase complex, ...
 
 
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Disease relevance of LPD1

 

High impact information on LPD1

 

Biological context of LPD1

  • We have shown for the LPD1 gene, encoding lipoamide dehydrogenase, that the coding sequence between +13 and +469 activated gene expression of an LPD1::lacZ fusion by up to sixfold in the presence of the upstream promoter [4].
  • Deletion and mutational analysis identified two downstream activation sites (DAS1 and DAS2) and two downstream repressor sites (DRS1 and DRS2) that influence the rate of LPD1 transcription rather than mRNA degradation or translation [4].
  • Therefore, the LPD1 gene appears to contain a transcriptional enhancer that lies 3' to the transcriptional start site, and which responds to carbon source [5].
  • The flanking region 5' to the LPD1 gene contains DNA sequences which show homology to known control sites found upstream of other yeast genes [6].
  • The LPD1 gene is present as a single copy in the yeast genome and is transcribed to give a polyadenylated mRNA species of approximately 2.0 kb [7].
 

Associations of LPD1 with chemical compounds

  • The LPD1 gene product is also required for cells to utilize glycine as sole nitrogen source [8].
  • Strains defective in LPD1 but transformed with the LPD1 gene on a high copy number vector exhibited elevated levels of the LPD1 transcript as well as increased lipoamide dehydrogenase activity when grown on glycerol [7].
  • The first, via branched chain alpha-ketoacid dehydrogenase to alpha-methylbutyryl-CoA, was eliminated because abolition of branched-chain alpha-ketoacid dehydrogenase in an lpd1 disruption mutant did not prevent the formation of active amyl alcohol [9].
  • This pathway is not required for the synthesis of isoamyl alcohol because abolition of branched-chain alpha-keto acid dehydrogenase activity in an lpd1 disruption mutant did not prevent the formation of isoamyl alcohol [10].
  • The first, via branched-chain alpha-ketoacid dehydrogenase to isobutyryl-CoA is not required for the synthesis of isobutyl alcohol because abolition of branched-chain alpha-ketoacid dehydrogenase activity in an lpd1 disruption mutant did not prevent the formation of isobutyl alcohol [11].
 

Other interactions of LPD1

 

Analytical, diagnostic and therapeutic context of LPD1

References

  1. Nucleotide sequence for yeast dihydrolipoamide dehydrogenase. Browning, K.S., Uhlinger, D.J., Reed, L.J. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  2. Autoantibody against dihydrolipoamide dehydrogenase, the E3 subunit of the 2-oxoacid dehydrogenase complexes: significance for primary biliary cirrhosis. Maeda, T., Loveland, B.E., Rowley, M.J., Mackay, I.R. Hepatology (1991) [Pubmed]
  3. 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]
  4. 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]
  5. A 3' transcriptional enhancer within the coding sequence of a yeast gene encoding the common subunit of two multi-enzyme complexes. Zaman, Z., Brown, A.J., Dawes, I.W. Mol. Microbiol. (1992) [Pubmed]
  6. The nucleotide sequence of the LPD1 gene encoding lipoamide dehydrogenase in Saccharomyces cerevisiae: comparison between eukaryotic and prokaryotic sequences for related enzymes and identification of potential upstream control sites. Ross, J., Reid, G.A., Dawes, I.W. J. Gen. Microbiol. (1988) [Pubmed]
  7. Cloning and characterization of the gene encoding lipoamide dehydrogenase in Saccharomyces cerevisiae. Roy, D.J., Dawes, I.W. J. Gen. Microbiol. (1987) [Pubmed]
  8. Genetics of the synthesis of serine from glycine and the utilization of glycine as sole nitrogen source by Saccharomyces cerevisiae. Sinclair, D.A., Dawes, I.W. Genetics (1995) [Pubmed]
  9. An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae. Dickinson, J.R., Harrison, S.J., Dickinson, J.A., Hewlins, M.J. J. Biol. Chem. (2000) [Pubmed]
  10. A 13C nuclear magnetic resonance investigation of the metabolism of leucine to isoamyl alcohol in Saccharomyces cerevisiae. Dickinson, J.R., Lanterman, M.M., Danner, D.J., Pearson, B.M., Sanz, P., Harrison, S.J., Hewlins, M.J. J. Biol. Chem. (1997) [Pubmed]
  11. An investigation of the metabolism of valine to isobutyl alcohol in Saccharomyces cerevisiae. Dickinson, J.R., Harrison, S.J., Hewlins, M.J. J. Biol. Chem. (1998) [Pubmed]
  12. 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]
  13. Isolation, characterization, and sequence analysis of a cDNA clone encoding L-protein, the dihydrolipoamide dehydrogenase component of the glycine cleavage system from pea-leaf mitochondria. Bourguignon, J., Macherel, D., Neuburger, M., Douce, R. Eur. J. Biochem. (1992) [Pubmed]
 
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