Deriving the Michaelis-Menten Equation from the Steady State · seed 1 · A4, ink-friendly. The answer key prints on its own page for grown-ups.

Where the rate equation comes from

Science · Biochemistry & Molecular Biology · ages 18-19
Name ______________________   Date ____________
  1. Where is Km on the rate curve?

    • The peak of the curve
    • The point where rate hits zero
    • The substrate level giving half the maximum
  2. What does the steady state assume about the complex?

    • It never forms at all
    • It forms as fast as it reacts
    • It grows without limit
  3. Raising substrate past saturation keeps raising the rate.

    Circle one:   True   False

  4. What sets Vmax?

    • Turnover per site times total enzyme
    • Substrate left at the end
    • The speed of product leaving only
  5. Km equals which mix of rate constants?

    • Binding over breakdown
    • Breakdown plus chemistry over binding
    • Chemistry alone
  6. When does the steady state hold?

    • Late, when substrate runs out
    • Early, while substrate far exceeds enzyme
    • Only with no enzyme present
  7. Why can extra substrate never pass Vmax?

    • Km blocks the way
    • Product pushes back harder
    • Sites are all busy already
  8. A mutant raises the chemistry rate but keeps binding fixed. What happens to Km?

    • It rises
    • It falls to zero
    • It stays exactly fixed
LightMySky · lightmysky.comW1-mt_BFp0fwZ8_i-s1

Answer key

For grown-ups. Fold this page away before handing over the rest.

Where the rate equation comes from W1-mt_BFp0fwZ8_i-s1

  1. The substrate level giving half the maximum · Km is defined as the substrate level at half Vmax.
  2. It forms as fast as it reacts · Formation and breakdown balance, holding the complex steady and low.
  3. False · Every site is already busy, so extra substrate finds no free site.
  4. Turnover per site times total enzyme · Vmax counts how fast all sites together turn over.
  5. Breakdown plus chemistry over binding · Km blends release and chemistry over the binding rate.
  6. Early, while substrate far exceeds enzyme · Early moments keep the complex small and constant.
  7. Sites are all busy already · Saturated sites leave no free room for extra substrate.
  8. It rises · Chemistry sits on top of the Km fraction, so faster chemistry raises it.
Worksheet · LightMySky