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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: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
- COFACTOR: Thiamine pyrophosphate.
- ENZYME REGULATION: E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit (By similarity).
- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
- SUBCELLULAR LOCATION: Mitochondrion matrix.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 13 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 1513 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: C97EEBF844085B19 [This is a checksum on the sequence] |
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