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MitoProteome Human Mitochondrial Protein Database
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Related Proteins
MT000185
UniProt Annotations
Entry Information
Gene Name
dihydrolipoamide S-acetyltransferase
Protein Entry
ODP2_HUMAN
UniProt ID
P10515
Species
Human
Comments
Comment type
Description
Catalytic Activity
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor
Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Note=Binds 2 lipoyl cofactors covalently.;
Disease
Note=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.
Disease
Pyruvate 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.
Function
The 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.
Interaction
P11177:PDHB; NbExp=7; IntAct=EBI-2959723, EBI-1035872;
Sequence Caution
Sequence=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};
Similarity
Belongs to the 2-oxoacid dehydrogenase family. {ECO:0000305}.
Similarity
Contains 2 lipoyl-binding domains. {ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000305}.
Subcellular Location
Mitochondrion matrix.
Subunit
Part 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}.
MitoProteome Human Mitochondrial Protein Database
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