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 | UniProt | Comment | Textmining |
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Escherichia coli | - |
- |
- |