Sometimes even enzymes are sated and have enough!
- saturation
- to plot against
- affinity
- to convert
- to enhance
- velocity
- to dissociate
- The active site catalyzes the reaction producing the product. This is the rate limiting step.
- The substrate binds at the binding site of the enzyme. This rate can vary and depends on the amount of substrate. The more substrate the quicker both meet.
- The enzyme-product complex dissociate to free product and enzyme.
- The two molecules form the enzyme-product complex.
- The enzyme is ready for the next catalysis reaction.
- The two molecules form the enzyme-substrate complex.
( ) The reaction rate of the enzymes starts off slowly. This is caused by a small amount of substrate. The affinity between both molecules is low.
( ) A lower KM means a high affinity between enzyme and substrate.
( ) A higher KM means a low affinity between enzyme and substrate.
( ) The conversion rate of the enzymes present cannot be further enhanced if the substrate amount is already very high. All enzymes are located in the enzyme-substrate complex, they are saturated.
( ) The reaction rate of the enzymes increases due to a higher amount of substrate. The affinity of both molecules becomes higher. The existing enzymes now convert more substrates into products in the same time.
( ) If the substrate concentration corresponds to the KM value, half of the originally present enzymes are present in the form of enzyme-substrate complexes. The other half is free.
( ) The Michaelis-Menten constant KM indicates the substrate concentration at which half the maximum reaction rate of the enzyme is reached.
( ) The half-maximum rate of substrate conversion is reached.
