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Enzyme Activity & Kinetics

អំពីការពិសោធន៍និម្មិតនេះ

Explore an enzyme’s active site and investigate substrate, temperature, pH and competitive inhibition with live rate curves.

អ្វីដែលសិស្សអាចស្វែងរកបាន

  • At 37 °C and pH 7, how does a competitive inhibitor change the rate as substrate increases?
  • Illustrative Michaelis–Menten model: v = Vmax[S]/(Km(1+I)+[S]), Km=2. Activity peaks at 37 °C and pH 7 using smooth response factors. Units are relative; this is not a particular enzyme or a reversible denaturation experiment. Binding artwork is schematic.

គោលបំណងសិក្សា

  1. 1At 37 °C and pH 7, how does a competitive inhibitor change the rate as substrate increases?

សំណួរដែលគ្រូតែងសួរ

At 37 °C and pH 7, how does a competitive inhibitor change the rate as substrate increases?

The inhibitor lowers the rate at a given substrate level. More substrate reduces its relative effect; both curves approach the same maximum.

About the model

Illustrative Michaelis–Menten model: v = Vmax[S]/(Km(1+I)+[S]), Km=2. Activity peaks at 37 °C and pH 7 using smooth response factors. Units are relative; this is not a particular enzyme or a reversible denaturation experiment. Binding artwork is schematic.

បញ្ចូលការពិសោធន៍និម្មិតនេះ

ដាក់វាចូលទៅក្នុង LMS ប្លក់ ឬគេហទំព័រថ្នាក់រៀនរបស់អ្នក — ឥតគិតថ្លៃ។

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