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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) (By similarity).
- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
- COFACTOR: Thiamine pyrophosphate (By similarity).
- 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 (By similarity).
- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
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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: 390 AA [This is the length of the unprocessed precursor] |
Molecular weight: 43366 Da [This is the MW of the unprocessed precursor] |
CRC64: 420CE38364BDB33C [This is a checksum on the sequence] |
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10 20 30 40 50 60
MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED
70 80 90 100 110 120
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA
130 140 150 160 170 180
HGFTFTRGLS VREILAELTG RKGGCAKGKG GSTHMYAKNF YRGNGIVGAQ VPLGAGIALA
190 200 210 220 230 240
CKYNGKDEVC LTLYGDGAAD QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST
250 260 270 280 290 300
DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS
310 320 330 340 350 360
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP
370 380 390
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS
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Q8HXW9 in FASTA format |
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