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Identification
NameDihydrolipoyl dehydrogenase, mitochondrial
Synonyms
  • Dihydrolipoamide dehydrogenase
  • Glycine decarboxylase complex subunit L
  • Lipoamide dehydrogenase component of pyruvate dehydrogenase complex
  • Pyruvate dehydrogenase complex E3 component
Gene NameLPD1
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionLipoamide dehydrogenase is a component of the alpha- ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine
Cellular LocationMitochondrion matrix
SMPDB Pathways
Pyruvate metabolismPW002447 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Citrate cycle (TCA cycle)ec00020 Map00020
Glycine, serine and threonine metabolismec00260 Map00260
Glycolysis / Gluconeogenesisec00010 Map00010
Pyruvate metabolismec00620 Map00620
Valine, leucine and isoleucine degradationec00280 Map00280
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00016GlycineShow
YMDB00045Coenzyme AShow
YMDB00110NADShow
YMDB00143NADHShow
YMDB00153Oxoglutaric acidShow
YMDB00175Pyruvic acidShow
YMDB00312Acetyl-CoAShow
YMDB00412NAD(+)Show
YMDB00423AmmoniumShow
YMDB004835,6,7,8-Tetrahydrofolic acidShow
YMDB00514Succinyl-CoAShow
YMDB00696S(8)-aminomethyldihydrolipoamideShow
YMDB00697lipoamideShow
YMDB00747S(8)-succinyldihydrolipoamideShow
YMDB00848(6R)-5,10-methylenetetrahydrofolic acidShow
YMDB00862hydronShow
YMDB00899DihydrolipoamideShow
YMDB00912Carbon dioxideShow
GO Classification
Component
cell part
intracellular part
cytoplasm
Function
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
FAD or FADH2 binding
oxidoreductase activity
oxidoreductase activity, acting on NADH or NADPH
oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
dihydrolipoyl dehydrogenase activity
catalytic activity
binding
Process
oxidation reduction
cellular process
cellular homeostasis
metabolic process
cell redox homeostasis
Gene Properties
Chromosome Locationchromosome 6
LocusYFL018C
Gene Sequence>1500 bp ATGTTAAGAATCAGATCACTCCTAAATAATAAGCGTGCCTTTTCGTCCACAGTCAGGACA TTGACCATTAACAAGTCACATGATGTAGTCATCATCGGTGGTGGCCCTGCTGGTTACGTG GCTGCTATCAAAGCTGCTCAATTGGGATTTAACACTGCATGTGTAGAAAAAAGAGGCAAA TTAGGCGGTACCTGTCTTAACGTTGGATGTATCCCCTCCAAAGCACTTCTAAATAATTCT CATTTATTCCACCAAATGCATACGGAAGCGCAAAAGAGAGGTATTGACGTCAACGGTGAT ATCAAAATTAACGTAGCAAACTTCCAAAAGGCTAAGGATGACGCTGTTAAGCAATTAACT GGAGGTATTGAGCTTCTGTTCAAGAAAAATAAGGTCACCTATTATAAAGGTAATGGTTCA TTCGAAGACGAAACGAAGATCAGAGTAACTCCCGTTGATGGGTTGGAAGGCACTGTCAAG GAAGACCACATACTAGATGTTAAGAACATCATAGTCGCCACGGGCTCTGAAGTTACACCC TTCCCCGGTATTGAAATAGATGAGGAAAAAATTGTCTCTTCAACAGGTGCTCTTTCGTTA AAGGAAATTCCCAAAAGATTAACCATCATTGGTGGAGGAATCATCGGATTGGAAATGGGT TCAGTTTACTCTAGATTAGGCTCCAAGGTTACTGTAGTAGAATTTCAACCTCAAATTGGT GCATCTATGGACGGCGAGGTTGCCAAAGCCACCCAAAAGTTCTTGAAAAAGCAAGGTTTG GACTTCAAATTAAGCACCAAAGTTATTTCTGCAAAGAGAAACGACGACAAGAACGTCGTC GAAATTGTTGTAGAAGATACTAAAACGAATAAGCAAGAAAATTTGGAAGCTGAAGTTTTG CTGGTTGCTGTTGGTAGAAGACCTTACATTGCTGGCTTAGGGGCTGAAAAGATTGGATTA GAAGTAGACAAAAGGGGACGCCTAGTCATTGATGACCAATTTAATTCCAAGTTCCCACAC ATTAAAGTGGTAGGAGATGTTACATTTGGTCCAATGCTGGCTCACAAAGCCGAAGAGGAA GGTATTGCAGCTGTCGAAATGTTGAAAACTGGTCACGGTCATGTCAACTATAACAACATT CCTTCGGTCATGTATTCTCACCCAGAAGTAGCATGGGTTGGTAAAACCGAAGAGCAATTG AAAGAAGCCGGCATTGACTATAAAATTGGTAAGTTCCCCTTTGCGGCCAATTCAAGAGCC AAGACCAACCAAGACACTGAAGGTTTCGTGAAGATTTTGATCGATTCCAAGACCGAGCGT ATTTTGGGGGCTCACATTATCGGTCCAAATGCCGGTGAAATGATTGCTGAAGCTGGCTTA GCCTTAGAATATGGCGCTTCCGCAGAAGATGTTGCTAGGGTCTGCCATGCTCATCCTACT TTGTCCGAAGCATTTAAGGAAGCTAACATGGCTGCCTATGATAAAGCTATTCATTGTTGA
Protein Properties
Pfam Domain Function
Protein Residues499
Protein Molecular Weight54009.69922
Protein Theoretical pI8.22
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Dihydrolipoyl dehydrogenase, mitochondrial MLRIRSLLNNKRAFSSTVRTLTINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGK LGGTCLNVGCIPSKALLNNSHLFHQMHTEAQKRGIDVNGDIKINVANFQKAKDDAVKQLT GGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHILDVKNIIVATGSEVTP FPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIG ASMDGEVAKATQKFLKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTKTNKQENLEAEVL LVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVVGDVTFGPMLAHKAEEE GIAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRA KTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPT LSEAFKEANMAAYDKAIHC
References
External Links
ResourceLink
Saccharomyces Genome Database LPD1
Uniprot IDP09624
Uniprot NameDLDH_YEAST
GenBank Gene IDD50617
Genebank Protein ID836736
PDB ID
1V59
General Reference
  • Browning, K. S., Uhlinger, D. J., Reed, L. J. (1988). "Nucleotide sequence for yeast dihydrolipoamide dehydrogenase." Proc Natl Acad Sci U S A 85:1831-1834.3279419
  • Ross, J., Reid, G. A., Dawes, I. W. (1988). "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." J Gen Microbiol 134:1131-1139.3058861
  • Murakami, Y., Naitou, M., Hagiwara, H., Shibata, T., Ozawa, M., Sasanuma, S., Sasanuma, M., Tsuchiya, Y., Soeda, E., Yokoyama, K., et, a. l. .. (1995). "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Nat Genet 10:261-268.7670463
  • Sinclair, D. A., Dawes, I. W. (1995). "Genetics of the synthesis of serine from glycine and the utilization of glycine as sole nitrogen source by Saccharomyces cerevisiae." Genetics 140:1213-1222.7498764
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Toyoda, T., Suzuki, K., Sekiguchi, T., Reed, L. J., Takenaka, A. (1998). "Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast." J Biochem 123:668-674.9538259