Literature summary for 1.2.5.1 extracted from

Bertagnolli, B.L.; Hager, L.P.
Activation of Escherichia coli pyruvate oxidase enhances the oxidation of hydroxyethylthiamin pyrophosphate (1991), J. Biol. Chem., 266, 10168-10173.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	the rate of decarboxylation of pyruvate to form CO2, and hydroxyethylthiamine diphosphate for both activated and unactivated forms of the enzyme is identical within experimental error. The pseudo-first order rate constant for the decarboxylation step is 60-80 per s. The pseudo-first order rate of oxidation of hydroxyethylthiamine diphosphate and concomitant enzyme-bound flavin reduction with unactivated enzyme is 2.85 per s and increases 145fold for lipid-activated enzyme to 413 per s and 61fold for the proteolytically activated enzyme to 173 per s. The rate of oxidation of enzyme-FADH is very fast for both unactivated and activated enzyme, being 1041 per s and 645 per s, respectively. The FAD reduction step is the rate-limiting step in the overall reaction for unactivated enzyme. Alternatively, the rate-limiting step in the overall reaction with the activated enzyme shifts to one of the partial steps in the decarboxylation reaction	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)