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Literature summary extracted from

  • Liu, S.; Gong, X.; Yan, X.; Peng, T.; Baker, J.C.; Li, L.; Robben, P.M.; Ravindran, S.; Andersson, L.A.; Cole, A.B.; Roche, T.E.
    Reaction Mechanism for Mammalian Pyruvate Dehydrogenase Using Natural Lipoyl Domain Substrates (2001), Arch. Biochem. Biophys., 386, 123-135.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.104 0.0248
-
 pyruvate
-
 Mammalia
1.2.1.104 0.052
-
 N-terminal lipoyl domain
-
 Mammalia
1.2.1.104 15
-
 N-acetyl-GDLLAEIETDK(lipoyl)-ATIG-amide
-
 Mammalia

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.104 Mammalia
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.104 0.035
-
 pyruvate as substrate, pyruvate dehydrogenase preparation with high activity Mammalia
1.2.1.104 0.16
-
 N-terminal lipoyl domain as substrate, pyruvate dehydrogenase preparation with high activity Mammalia

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.104 pyruvate + N-acetyl-GDLLAEIETDK(lipoyl)-ATIG-amide
-
 Mammalia ?
-
 r
1.2.1.104 pyruvate + N-terminal lipoyl domain
-
 Mammalia ?
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.104 5
-
 N-acetyl-GDLLAEIETDK(lipoylated)ATIG-amide
-
 Mammalia
1.2.1.104 26.3
-
 N-terminal lipoyl domain
-
 Mammalia
1.2.1.104 70
-
 N-terminal lipoyl domain pyruvate dehydrogenase preparation with high activity Mammalia