Literature summary for 1.2.5.1 extracted from

Mather, M.W.; Gennis, R.B.
Kinetic studies of the lipid-activated pyruvate oxidase flavoprotein of Escherichia coli (1985), J. Biol. Chem., 260, 16148-16155.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	the unactivated form of enzyme is markedly hysteretic. At low substrate concentration, there is an initial acceleration in enzyme turnover due to slow interconversion between two forms of the enzyme, one with low turnover and one which rapidly turns over. During turnover, even in the absence of lipid activators, some of the enzyme converts to the rapid-turnover form. This slow interconversion precludes a steady state from being established. Lipid activators shift the equilibrium to favor the rapid turnover form of the enzyme. Once the enzyme is locked into an activated conformation, the hysteresis is no longer observed. Activation results in both increased rates of electron transfer into and out of the flavin	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)