LMPD Database

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LMP007331

UniProt Annotations

Entry Information
Gene Namedihydrolipoyllysine-residue acetyltransferase
Protein EntryODP2_YEAST
UniProt IDP12695
SpeciesYeast (S288c)
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 1 lipoyl cofactor covalently.;
FunctionThe pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). {ECO:0000269|PubMed:7030741}.
MiscellaneousPresent with 5440 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
MiscellaneousThe E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.
SimilarityBelongs to the 2-oxoacid dehydrogenase family. {ECO:0000305}.
SimilarityContains 1 lipoyl-binding domain. {ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000305}.
Subcellular LocationMitochondrion matrix {ECO:0000269|PubMed:14562095}.
SubunitEukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds. {ECO:0000269|PubMed:7030741}.