The Michaelis–Menten rate equation for enzyme reactions is typically written as the rate of formation of product (Eq. 1a).
This equation implies that 1/rate (where rate is the rate of formation of product) depends linearly on the inverse of the substrate concentration [S]. This relation allows K_M to be determined.
Derive this equation and sketch 1/rate against 1/[S]. Label the axes, the y-intercept, and the slope with their corresponding expressions in terms of K_M and [S].

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Rate of formation of product = K₂ [E]0[S] KM + [S] (1a)