[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-43; ALA-318 AND ASN-451.
TISSUE=Kidney;
Totoki Y.,
Toyoda A.,
Takeda T.,
Sakaki Y.,
Tanaka A.,
Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04632; PubMed=16554811 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor T.D.,
Noguchi H.,
Totoki Y.,
Toyoda A.,
Kuroki Y.,
Dewar K.,
Lloyd C.,
Itoh T.,
Takeda T.,
Kim D.-W.,
She X.,
Barlow K.F.,
Bloom T.,
Bruford E.,
Chang J.L.,
Cuomo C.A.,
Eichler E.,
FitzGerald M.G.,
Jaffe D.B., ![]()
LaButti K.,
Nicol R.,
Park H.-S.,
Seaman C.,
Sougnez C.,
Yang X.,
Zimmer A.R.,
Zody M.C.,
Birren B.W.,
Nusbaum C.,
Fujiyama A.,
Hattori M.,
Rogers J.,
Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene identification.";
Nature 440:497-500(2006).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] OF 33-647.
TISSUE=Placenta;
DOI=10.1073/pnas.85.19.7317; PubMed=3174635 [NCBI, ExPASy, EBI, Israel, Japan]
Coppel R.L.,
McNeilage L.J.,
Surh C.D.,
van de Water J.,
Spithill T.W.,
Whittingham S.,
Gershwin M.E.;
"Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase.";
Proc. Natl. Acad. Sci. U.S.A. 85:7317-7321(1988).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] OF 73-647.
TISSUE=Liver;
DOI=10.1016/0014-5793(88)80337-5; PubMed=3191998 [NCBI, ExPASy, EBI, Israel, Japan]
Thekkumkara T.J.,
Ho L.,
Wexler I.D.,
Pon G.,
Liu T.,
Patel M.S.;
"Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex.";
FEBS Lett. 240:45-48(1988).
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[5]
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IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J.,
Superti-Furga G.,
Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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[6]
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STRUCTURE BY NMR OF 214-315.
PubMed=9649469 [NCBI, ExPASy, EBI, Israel, Japan]
Howard M.J.,
Fuller C.,
Broadhurst R.W.,
Perham R.N.,
Tang J.G.,
Quinn J.,
Diamond A.G.,
Yeaman S.J.;
"Three-dimensional structure of the major autoantigen in primary biliary cirrhosis.";
Gastroenterology 115:139-146(1998).
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[7]
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INVOLVEMENT IN PYRUVATE DEHYDROGENASE E2 DEFICIENCY.
DOI=10.1002/ana.20550; PubMed=16049940 [NCBI, ExPASy, EBI, Israel, Japan]
Head R.A.,
Brown R.M.,
Zolkipli Z.,
Shahdadpuri R.,
King M.D.,
Clayton P.T.,
Brown G.K.;
"Clinical and genetic spectrum of pyruvate dehydrogenase deficiency: dihydrolipoamide acetyltransferase (E2) deficiency.";
Ann. Neurol. 58:234-241(2005).
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[8]
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STRUCTURE BY NMR OF 92-186.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-058, a lipoyl domain of human 2-oxoacid dehydrogenase.";
Submitted (OCT-2006) to the PDB data bank.
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- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.
- COFACTOR: Binds 2 lipoyl cofactors covalently.
- SUBUNIT: 20 to 30 alpha(2)-beta(2) tetramers of E1 + 6 homodimers of E3 + 60 copies of E2.
- SUBCELLULAR LOCATION: Mitochondrion matrix.
- 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.
- DISEASE: Defects in DLAT are the cause of pyruvate dehydrogenase E2 deficiency [MIM:245348]; also known as lactic acidemia due to defect of E2 lipoyl transacetylase of the pyruvate dehydrogenase complex. 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.
- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
- SIMILARITY: Contains 2 lipoyl-binding domains.
- SEQUENCE CAUTION:
- Sequence=AAA62253.1; Type=Frameshift; Positions=449, 451, 455;
- Sequence=AAA62253.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part
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