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Literature summary for 2.3.1.12 extracted from

  • Reed, L.J.; Yeaman, S.J.
    Pyruvate dehydrogenase (1987), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 18, 77-95.
No PubMed abstract available

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
60 * 52000 Mammalia
3100000
-
-
Mammalia

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dihydrolipoamide + acetyl-CoA Mammalia
-
S-acetyldihydrolipoamide + CoA
-
?
dihydrolipoamide + acetyl-CoA Geobacillus stearothermophilus
-
S-acetyldihydrolipoamide + CoA
-
?

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-
Mammalia
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein 1 lipoyl domain Mammalia

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + acetyl-CoA
-
Mammalia S-acetyldihydrolipoamide + CoA
-
?
dihydrolipoamide + acetyl-CoA
-
Geobacillus stearothermophilus S-acetyldihydrolipoamide + CoA
-
?

Subunits

Subunits Comment Organism
polymer 60 * 52000 Mammalia
polymer stoichiometry of pyruvate dehydrogenase complexes Mammalia
polymer stoichiometry of pyruvate dehydrogenase complexes Geobacillus stearothermophilus
polymer 60 subunits Geobacillus stearothermophilus