On times , the quasi-steady-state approximation sets
The second equation gives
In the first equation the terms then cancel, leaving
Solving these two equations gives
Since ,
At small substrate concentration this allosteric rate is quadratic, , so its graph leaves the origin with zero slope. At large it saturates at . A Michaelis-Menten equation also saturates, but its rate is linear near the origin. The allosteric curve is therefore more sigmoidal:
This is the quasi-steady rate law for a two-substrate allosteric enzyme.

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