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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617;
PubMed=3292237 [NCBI, ExPASy, EBI, Israel, Japan]
Hanemaaijer R.,
Janssen A.,
de Kok A.,
Veeger C.;
"The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis.";
Eur. J. Biochem. 174:593-599(1988).
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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.
- SUBUNIT: Homodimer.
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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: 45 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 4957 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: C2929BB637D1B032 [This is a checksum on the sequence] |
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10 20 30 40
EVDRYWVVLA ALEALADRGD IEAKVVAEAI AKFGIDPDKR NPLDC
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P10801 in FASTA format |
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