Linked Life Data

CPATH-93172

Source:http://cbio.mskcc.org/cpath#CPATH-93172

Statements in which the resource exists.
SubjectPredicateObjectContext
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cpath:CPATH-93172http://www.biopax.org/relea...Pyruvate dehydrogenase E1 component subunit alpha, mitochondriallld:biogrid
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cpath:CPATH-93172http://www.biopax.org/relea...Pyruvate dehydrogenase complex component E1 alphalld:biogrid
cpath:CPATH-93172http://www.biopax.org/relea...FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). COFACTOR: Thiamine pyrophosphate. ENZYME REGULATION: E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit. SUBUNIT: Pyruvate 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. SUBCELLULAR LOCATION: Mitochondrion matrix. MISCELLANEOUS: Present with 100000 molecules/cell in log phase SD medium. SEQUENCE CAUTION: Sequence=AAB64705.1; Type=Erroneous initiation; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.lld:biogrid
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