Literature summary for 1.2.4.1 extracted from

Saumweber, H.; Binder, R.; Bisswanger, H.
Pyruvate dehydrogenase component of the pyruvate dehydrogenase complex from Escherichia coli K12. Purification and characterization (1981), Eur. J. Biochem., 114, 407-411.

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Inhibitors

Inhibitors	Comment	Organism	Structure
Fluoropyruvate	competitive with respect to pyruvate, both free and complex bound enzyme behave in the same manner	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	sigmoidal dependence on the concentration of pyruvate, Hill-coefficient: 1.85	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
100000	-	2 * 100000, SDS-PAGE	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1791	-	activity after reassociation of the purified enzyme with EC 2.3.1.12 and EC 1.8.1.4	Escherichia coli

Subunits

Subunits	Comment	Organism
dimer	2 * 100000, SDS-PAGE	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
additional information	-	value for pyruvate dehydrogenase complex: 45°C	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	7.5	-	Escherichia coli

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.018	-	Fluoropyruvate	-	Escherichia coli

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Release 2023.1 (January 2023)