chemistry / Chemistry of Life / free

Biochemistry

Understand the reactions that let cells store, move, and use energy.

Follow the cause1 / 3

A substrate finds a selective site. Shape, charge, hydrogen bonds, and hydrophobic interactions make some encounters productive.

enzyme actionv = 49% of Vmax · binding
Focus the idea
Substrate concentration changes enzyme velocityA substrate concentration of 58 µM with 18 µM of a competitive inhibitor gives a velocity of 49 percent of Vmax; the apparent Kₘ is 61 µM.v = Vmax[S]/(Kₘ(1 + [I]/Kᵢ) + [S])Vmax[S] (µM) →velocity ↑faint: no inhibitor
substrate58 µM
apparent Kₘ61 µM
Vmax100% (unchanged)
velocity49% of Vmax

More substrate raises encounter frequency until active sites approach saturation. A competitive inhibitor raises the apparent Kₘ from 32 to 61 µM but leaves Vmax at 100%, so enough substrate can still outcompete it.

The Michaelis–Menten curve is a simplified steady-state model with Kₘ = 32 µM and Kᵢ = 20 µM for a competitive inhibitor. Real enzymes can have multiple substrates, cooperativity, allostery, crowding, and regulation.

04 / PRACTICE

Make the chemistry yours.

0 / 3 checked

Answer from the model, then use the explanation to connect the particle picture to the chemical rule.

CHECK 1 / 3

Why does enzyme velocity plateau at high substrate concentration?