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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 (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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Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 397 AA [This is the length of the unprocessed precursor] |
Molecular weight: 43792 Da [This is the MW of the unprocessed precursor] |
CRC64: 27FB6410B0EA8513 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSLFARQLQS LTASGIRTQQ VRLASTEVSF HTKPCKLHKL DNGPNTSVTL NREDALKYYR
70 80 90 100 110 120
DMQVIRRMES AAGNLYKEKK IRGFCHLYSG QEACAVGMKA AMTEGDAVIT AYRCHGWTWL
130 140 150 160 170 180
LGATVTEVLA ELTGRVAGNV HGKGGSMHMY TKNFYGGNGI VGAQQPLGAG VALAMKYREQ
190 200 210 220 230 240
KNVCVTLYGD GAANQGQLFE ATNMAKLWDL PVLFVCENNG FGMGTTAERS SASTEYYTRG
250 260 270 280 290 300
DYVPGIWVDG MDILAVREAT KWAKEYCDSG KGPLMMEMAT YRYHGHSMSD PGTSYRTREE
310 320 330 340 350 360
IQEVRKTRDP ITGFKDRIIT SSLATEEELK AIDKEVRKEV DEALKIATSD GVLPPEALYA
370 380 390
DIYHNTPAQE IRGATIDETI VQPFKTSADV LKSIGRA
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P52899 in FASTA format |
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