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MGP000837

UniProt Annotations

Entry Information
Gene Namedihydrolipoamide S-acetyltransferase
Protein EntryODP2_HUMAN
UniProt IDP10515
SpeciesHuman
Comments
Comment typeDescription
Catalytic ActivityAcetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CofactorName=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Note=Binds 2 lipoyl cofactors covalently.;
DiseaseNote=Primary biliary cirrhosis is a chronic, progressive cholestatic liver disease characterized by the presence of antimitochondrial autoantibodies in patients' serum. It manifests with inflammatory obliteration of intra-hepatic bile duct, leading to liver cell damage and cirrhosis. Patients with primary biliary cirrhosis show autoantibodies against the E2 component of pyruvate dehydrogenase complex.
DiseasePyruvate dehydrogenase E2 deficiency (PDHE2 deficiency) [MIM:245348]: Pyruvate dehydrogenase (PDH) deficiency is a major cause of primary lactic acidosis and neurological dysfunction in infancy and early childhood. In this form of PDH deficiency episodic dystonia is the major neurological manifestation, with other more common features of pyruvate dehydrogenase deficiency, such as hypotonia and ataxia, being less prominent. {ECO:0000269|PubMed:16049940}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionThe pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
InteractionP11177:PDHB; NbExp=7; IntAct=EBI-2959723, EBI-1035872;
Sequence CautionSequence=AAA62253.1; Type=Frameshift; Positions=449, 451, 455; Evidence={ECO:0000305}; Sequence=AAA62253.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
SimilarityBelongs to the 2-oxoacid dehydrogenase family. {ECO:0000305}.
SimilarityContains 2 lipoyl-binding domains. {ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000305}.
Subcellular LocationMitochondrion matrix.
SubunitPart of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2 and PDK3. {ECO:0000269|PubMed:14638692, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:18387944}.
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