{"ymdb_id":"YMDB00899","created_at":"2011-05-29T19:02:46.000Z","updated_at":"2016-09-08T18:36:02.000Z","name":"Dihydrolipoamide","cas":"3884-47-7","state":"Solid","melting_point":"","description":"Dihydrolipoamide is an intermediate in glycolysis/gluconeogenesis, citrate cycle, alanine, aspartate and pyruvate metabolism, and valine, leucine and isoleucine degradation. It is converted to lipoamide via the enzyme dihydrolipoamide dehydrogenase [EC:1.8.1.4]. Dihydrolipoamide is also a substrate of enzyme Acyltransferases [EC 2.3.1.-]. [KEGG]","experimental_water_solubility":"","experimental_logp_hydrophobicity":"","location":"mitochondrion","synthesis_reference":"Weitzman, P. D. J.; Hewson, Janet K.; Parker, M. G.  Preparation of dihydrolipoamide by electrolytic reduction.    FEBS Letters  (1974),  43(1),  101-3.","chebi_id":"17694","hmdb_id":"HMDB00985","kegg_id":"C00579","pubchem_id":"663","cs_id":"643","foodb_id":null,"wikipedia_link":"Dihydrolipoamide","biocyc_id":"DIHYDROLIPOAMIDE","iupac":"6,8-disulfanyloctanimidic acid","traditional_iupac":"dihydrothioctamide","logp":"1.438392507588704","pka":"9.850896014465793","alogps_solubility":"9.92e-02 g/l","alogps_logp":"2.22","alogps_logs":"-3.32","acceptor_count":"2","donor_count":"4","rotatable_bond_count":"7","polar_surface_area":"44.08","refractivity":"68.6954","polarizability":"23.767533674169556","formal_charge":"0","physiological_charge":"0","pka_strongest_basic":"8.781980224833603","pka_strongest_acidic":"6.676732176319095","bioavailability":"1","number_of_rings":"0","rule_of_five":"1","ghose_filter":"1","veber_rule":"0","mddr_like_rule":"0","synonyms":["6,8-bis-sulfanyloctanamide","6,8-dimercapto-Octanamide","6,8-dimercaptooctanamide","6,8-disulfanyloctanamide","dihydrolipoamide","Dihydrothioctamide"],"pathways":[],"growth_conditions":[],"references":[{"pubmed_id":18846089,"citation":"Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). \"A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology.\" Nat Biotechnol 26:1155-1160."},{"pubmed_id":3050999,"citation":"Niu, X. D., Browning, K. S., Behal, R. H., Reed, L. J. (1988). \"Cloning and nucleotide sequence of the gene for dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae.\" Proc Natl Acad Sci U S A 85:7546-7550."},{"pubmed_id":2178788,"citation":"Ruttkay-Nedecky, B., Subik, J. (1990). \"The OGD1 gene, affecting 2-oxoglutarate dehydrogenase in S. cerevisiae, is closely linked to HIS5 on chromosome IX.\" Curr Genet 17:85-88."}],"proteins":[{"created_at":"2011-05-24T20:14:31.000Z","updated_at":"2011-05-27T14:56:00.000Z","name":"Dihydrolipoyl dehydrogenase, mitochondrial","uniprot_id":"P09624","uniprot_name":"DLDH_YEAST","enzyme":true,"transporter":false,"gene_name":"LPD1","num_residues":499,"molecular_weight":"54009.69922","theoretical_pi":"8.22","general_function":"Involved in oxidoreductase activity","specific_function":"Lipoamide 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","reactions":[{"id":2306,"direction":"\u003e","locations":"Mitochondrion matrix","altext":"Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH.","export":false,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":"1V59","cellular_location":"Mitochondrion matrix","genbank_gene_id":"D50617","genbank_protein_id":"836736","gene_card_id":"LPD1","chromosome_location":"chromosome 6","locus":"YFL018C","synonyms":["Dihydrolipoamide dehydrogenase","Glycine decarboxylase complex subunit L","Lipoamide dehydrogenase component of pyruvate dehydrogenase complex","Pyruvate dehydrogenase complex E3 component"],"enzyme_classes":["1.8.1.4"],"go_classes":[{"category":"Component","description":" cell part"},{"category":"Component","description":" intracellular part"},{"category":"Component","description":" cytoplasm"},{"category":"Function","description":" binding"},{"category":"Function","description":" nucleoside binding"},{"category":"Function","description":" purine nucleoside binding"},{"category":"Function","description":" adenyl nucleotide binding"},{"category":"Function","description":" FAD or FADH2 binding"},{"category":"Function","description":" oxidoreductase activity"},{"category":"Function","description":" oxidoreductase activity, acting on NADH or NADPH"},{"category":"Function","description":" oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor"},{"category":"Function","description":" dihydrolipoyl dehydrogenase activity"},{"category":"Function","description":" catalytic activity"},{"category":"Process","description":" oxidation reduction"},{"category":"Process","description":" cellular process"},{"category":"Process","description":" cellular homeostasis"},{"category":"Process","description":" metabolic process"},{"category":"Process","description":" cell redox homeostasis"}],"pfams":[{"name":"Pyr_redox","identifier":"PF00070"},{"name":"Pyr_redox_2","identifier":"PF07992"},{"name":"Pyr_redox_dim","identifier":"PF02852"}],"pathways":[{"name":"Glycolysis / Gluconeogenesis","kegg_map_id":"00010"},{"name":"Citrate cycle (TCA cycle)","kegg_map_id":"00020"},{"name":"Glycine, serine and threonine metabolism","kegg_map_id":"00260"},{"name":"Valine, leucine and isoleucine degradation","kegg_map_id":"00280"},{"name":"Pyruvate metabolism","kegg_map_id":"00620"}],"gene_sequence":"ATGTTAAGAATCAGATCACTCCTAAATAATAAGCGTGCCTTTTCGTCCACAGTCAGGACATTGACCATTAACAAGTCACATGATGTAGTCATCATCGGTGGTGGCCCTGCTGGTTACGTGGCTGCTATCAAAGCTGCTCAATTGGGATTTAACACTGCATGTGTAGAAAAAAGAGGCAAATTAGGCGGTACCTGTCTTAACGTTGGATGTATCCCCTCCAAAGCACTTCTAAATAATTCTCATTTATTCCACCAAATGCATACGGAAGCGCAAAAGAGAGGTATTGACGTCAACGGTGATATCAAAATTAACGTAGCAAACTTCCAAAAGGCTAAGGATGACGCTGTTAAGCAATTAACTGGAGGTATTGAGCTTCTGTTCAAGAAAAATAAGGTCACCTATTATAAAGGTAATGGTTCATTCGAAGACGAAACGAAGATCAGAGTAACTCCCGTTGATGGGTTGGAAGGCACTGTCAAGGAAGACCACATACTAGATGTTAAGAACATCATAGTCGCCACGGGCTCTGAAGTTACACCCTTCCCCGGTATTGAAATAGATGAGGAAAAAATTGTCTCTTCAACAGGTGCTCTTTCGTTAAAGGAAATTCCCAAAAGATTAACCATCATTGGTGGAGGAATCATCGGATTGGAAATGGGTTCAGTTTACTCTAGATTAGGCTCCAAGGTTACTGTAGTAGAATTTCAACCTCAAATTGGTGCATCTATGGACGGCGAGGTTGCCAAAGCCACCCAAAAGTTCTTGAAAAAGCAAGGTTTGGACTTCAAATTAAGCACCAAAGTTATTTCTGCAAAGAGAAACGACGACAAGAACGTCGTCGAAATTGTTGTAGAAGATACTAAAACGAATAAGCAAGAAAATTTGGAAGCTGAAGTTTTGCTGGTTGCTGTTGGTAGAAGACCTTACATTGCTGGCTTAGGGGCTGAAAAGATTGGATTAGAAGTAGACAAAAGGGGACGCCTAGTCATTGATGACCAATTTAATTCCAAGTTCCCACACATTAAAGTGGTAGGAGATGTTACATTTGGTCCAATGCTGGCTCACAAAGCCGAAGAGGAAGGTATTGCAGCTGTCGAAATGTTGAAAACTGGTCACGGTCATGTCAACTATAACAACATTCCTTCGGTCATGTATTCTCACCCAGAAGTAGCATGGGTTGGTAAAACCGAAGAGCAATTGAAAGAAGCCGGCATTGACTATAAAATTGGTAAGTTCCCCTTTGCGGCCAATTCAAGAGCCAAGACCAACCAAGACACTGAAGGTTTCGTGAAGATTTTGATCGATTCCAAGACCGAGCGTATTTTGGGGGCTCACATTATCGGTCCAAATGCCGGTGAAATGATTGCTGAAGCTGGCTTAGCCTTAGAATATGGCGCTTCCGCAGAAGATGTTGCTAGGGTCTGCCATGCTCATCCTACTTTGTCCGAAGCATTTAAGGAAGCTAACATGGCTGCCTATGATAAAGCTATTCATTGTTGA","protein_sequence":"MLRIRSLLNNKRAFSSTVRTLTINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTCLNVGCIPSKALLNNSHLFHQMHTEAQKRGIDVNGDIKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHILDVKNIIVATGSEVTPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAYDKAIHC"}]}