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ChemBench
The central equation of enzyme kinetics — how fast an enzyme works depends on how much substrate is available.
At low substrate concentrations, velocity increases nearly linearly — the enzyme has plenty of free active sites. As substrate concentration rises, the enzyme saturates and velocity plateaus at Vmax. The Km value is the substrate concentration at which velocity is exactly half of Vmax, and it measures the enzyme's affinity for its substrate.
A low Km means the enzyme binds substrate tightly (high affinity) and reaches half-max velocity at low concentrations. Drug designers target enzymes by comparing their drug's binding affinity to the natural substrate's Km — competitive inhibitors effectively increase the apparent Km.
Molar mass of any chemical formula (e.g. H2O, C6H12O6, Ca(OH)2).
OpenPercent composition of an element within a chemical formula.
OpenSimplest whole-number ratio formula from elemental masses or percentages.
OpenPercent yield from actual and theoretical reaction yields.
OpenReaction velocity
66.667
What you entered
Km + [S]
5 + 10= 15v = Vmax × [S] ÷ (Km + [S])
100 × 10 ÷ 15= 66.6667 mol/L/sFraction of Vmax
66.6667 ÷ 100 × 100= 66.6667%Result
Reaction velocity: 66.667
At [S] = 10 mM (Km = 5 mM), the enzyme operates at 66.7% of its maximum velocity (v = 66.667 μmol/min).