Which phenomenon limits reaction rate when an enzyme's Michaelis constant (Km) is significantly higher than substrate concentration?

💡 Explanation

When Km >> [S], the enzyme active sites are far from saturated because relatively little substrate is bound, meaning achieving maximal velocity requires much higher substrate concentrations to overcome substrate affinity. Therefore maximum velocity becomes harder to reach, rather than product inhibition, diffusion limitations, or conformational changes that typically happen at MUCH higher substrate concentrations or later enzyme phases.

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