Suppose an allosterically regulated enzyme had a mutation th

Suppose an allosterically regulated enzyme had a mutation that caused the R:T ratio to be 100:1 in the absence of substrate. How would the rate of this reaction respond to substrate concentration?

Solution

Allosterically regulated enzyme is a regulatory enzyme that binds a effector molecule at a site other than enzyme active site.The T state is the tense state which has low affinity and activity and R is the relaxed state which has high affinty and activity.If an allosterically enzyme had a mutation in the absence of substrate that reversed the T/R ratio. And the rate of reaction(V) and substrate concentration would show simple Michaels- Menten kinetics.

i.e. V=V_max+[s] / K_m+[s].