KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
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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 | UniProt | Comment | Textmining |
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Escherichia coli | - |
- |
- |