Michaelis-Menten Tool

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Enzymes accelerate the rates of biochemical reactions. One of the most common schemes for describing enzyme kinetics involving a single substrate is the Michaelis-Menten scheme.

This interactive tool will help you understand Michaelis-Menten kinetics and observe the Michaelis-Menten equation at work.

k_cat measures the number of substrate molecules "turned over" per enzyme molecule in one second. The k_catis also considered the "turnover number."

[E]_tmeasures the total enzyme concentration.

K_Mis the Michaelis constant, which is the substrate concentration at which the velocity is half of maximum velocity.

Use the sliders to change concentrations of k_cat, [E]_t, and K_M.

The resulting graph shows reaction velocity, V, as a function of substrate concentration [S].

Maximal velocity, V_max , is approached asymptotically. The Michaelis constant, K_Mis the substrate concentration yielding a velocity of V_max/2.

k_cat in sec-1	[E]_tin M, where “M” is molar	K_Min M