LMPD Database

LMP006945

UniProt Annotations

Entry Information
Gene Namepyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha
Protein EntryODPA_YEAST
UniProt IDP16387
SpeciesYeast (S288c)
Comments
Comment typeDescription
Catalytic ActivityPyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CofactorName=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
Enzyme RegulationE1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.
FunctionThe pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
MiscellaneousPresent with 100000 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
PtmPhosphorylated at Ser-313 by pyruvate dehydrogenase kinases PKP1 (PDK1) and PKP2 (PDK2), and dephosphorylated by pyruvate dehydrogenase phosphatases PTC5 and PTC6. {ECO:0000269|PubMed:15665377, ECO:0000269|PubMed:17330950, ECO:0000269|PubMed:17761666, ECO:0000269|PubMed:18180296, ECO:0000269|PubMed:18407956, ECO:0000269|PubMed:19779198}.
Sequence CautionSequence=AAB64705.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Subcellular LocationMitochondrion matrix.
SubunitPyruvate dehydrogenase (E1) is a tetramer of 2 alpha and 2 beta subunits. Eukaryotic 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.