Michaelis–Menten kinetics template

The v₀ against [S] hyperbola with Vmax and Km (the [S] at ½Vmax) marked, the Lineweaver–Burk plot (slope Km/Vmax, intercepts 1/Vmax and −1/Km), and the E + S ⇌ ES → E + P scheme with kcat and kcat/Km.

What the template shows

• Initial rate against [S] is a rectangular hyperbola; its double reciprocal is a straight line that gives Km and Vmax from the intercepts
• The rate law and its linear form
• Curves drawn for Km = 1 and Vmax = 1 (arbitrary units)
• Rate against substrate concentration
• first order at low [S], zero order at saturation
• Lineweaver–Burk (double-reciprocal) plot
• slope = Km/Vmax
• 1/v₀ = (Km/Vmax)·(1/[S]) + 1/Vmax
• Where Km and Vmax come from
• k₁ (binding), k₋₁ (release), kcat (catalysis)
• Briggs–Haldane steady state: d[ES]/dt ≈ 0, [S] ≫ [E]
• kcat = Vmax / [E]ₜ (turnover number) · kcat/Km = specificity constant
• Km is the substrate concentration that gives half the maximum rate. It equals the dissociation constant of ES only when kcat ≪ k₋₁.
• Vmax = kcat[E]ₜ is reached when every enzyme molecule is saturated with substrate; kcat/Km (up to about 10⁸–10⁹ M⁻¹ s⁻¹, the diffusion limit) measures catalytic efficiency.
• The double-reciprocal plot stretches the least accurate low-[S] points, so Km and Vmax are now fitted to v₀ against [S] directly; the plot is still the clearest way to tell inhibitors apart.

Drawn with 194 shapes – every one editable in MolDraw.

Sources

• Nelson & Cox, Lehninger Principles of Biochemistry, 8th ed., 2021, ch. 6 Textbook
• Berg, Tymoczko, Gatto & Stryer, Biochemistry, 9th ed., 2019 Textbook
• Michaelis & Menten, Biochem. Z. 1913, 49, 333; English translation: Johnson & Goody, Biochemistry 2011, 50, 8264 Original paper
• Briggs & Haldane, Biochem. J. 1925, 19, 338 Original paper