Enzyme Properties

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  • Enzyme Properties
    • Non-competitive Inhibitors
      • the inhibitor alters the shape of the enzymes active site so substrates no longer fit
      • this means the enzyme can no longer function
      • attach themselves to the enzyme at a site which is not the active site
    • Effect of Temperature
      • the enzyme and substrate molecules come together more frequently
      • the molecules move around more rapidly and collide with each other
      • a rise in temperature causes a rise in KINETIC ENERGY
      • shown as a rising curve on a graph
      • the rise in temperature also causes bonds to break, changing the shape of the active site
      • at 60 degrees the enzymes are denatured
    • Competitive Inhibitors
      • they compete with the substrate for available active sites
      • they have a molecular shape that is similar to the substrate
      • bind to the active site of the enzyme
      • if substrate concentration increases, the effect of the inhibitor is reduced
    • Effect of pH
      • a change in pH can cause the bonds to break and change the enzymes shape
      • if the substrate no longer fits the enzyme has been denatured
      • a change in pH alters the charge of the active site so the enzyme-substrate complex cannot be formed
      • small changes in the pH change the active site
      • each enzyme has an optimum pH which it works the fastest
    • Effect of Substrate Concentration
      • as more substrate is added, more active sites are filled
      • at low substrate levels there are a limited amount of substrate molecules to collide
      • the rate of reaction is at its optimum when all the active sites are working as fast as they can
      • if substrate increases the rate of reaction increases

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