DLAT
Function
As part of the pyruvate dehydrogenase complex, catalyzes the transfers of an acetyl group to a lipoic acid moiety (Probable). The pyruvate dehydrogenase complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable).
Involvement in disease
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.
Pyruvate dehydrogenase E2 deficiency
PDHE2 deficiency
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.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
Delipoylated at Lys-132 and Lys-259 by SIRT4, delipoylation decreases the PHD complex activity.
Sequence Similarities
Belongs to the 2-oxoacid dehydrogenase family.
Cellular localization
- Mitochondrion matrix
Alternative names
DLTA, DLAT, 70 kDa mitochondrial autoantigen of primary biliary cirrhosis, Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, M2 antigen complex 70 kDa subunit, Pyruvate dehydrogenase complex component E2, PBC, PDC-E2, PDCE2