dAn allosteric enzyme that follows the concerted mechanism (MWC model) has a T/R ratio of 300 in the absence of substrate. E Suppose that a mutation reversed the ratio. ENor tha i he in active tom of the man an Tis i les ate form the crys
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Turned upside down. An allosteric enzyme that follows the concerted model has a T/R ratio of 300 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and the substrate concentration?
No T. What would be the effect of a mutation in an allosteric enzyme that resulted in a T/R ratio of 0?
Allosteric switching. A substrate binds 100 times as tightly to the $R$ state of an allosteric enzyme as to its T state. Assume that the concerted (MWC) model applies to this enzyme. (See equations for the Concerted Model in the Appendix to Chapter $7 .$ ) (a) By what factor does the binding of one substrate molecule per enzyme molecule alter the ratio of the concentrations of enzyme molecules in the $\mathrm{R}$ and $\mathrm{T}$ states? (b) Suppose that $L,$ the ratio of $[\mathrm{T}]$ to $[\mathrm{R}]$ in the absence of substrate, is $10^{7}$ and that the enzyme contains four binding sites for substrate. What is the ratio of enzyme molecules in the $\mathrm{R}$ state to those in the T state in the presence of saturating amounts of substrate, assuming that the concerted model is obeyed?
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