Literature summary for 1.2.1.104 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.

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KM Value [mM]

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

Organism

Organism	UniProt	Comment	Textmining
Mammalia	-	-	-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

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Release 2023.1 (January 2023)