• Michaelis-Menten Kinetics
  • Julia Schulz
  • 30.06.2020
  • Allgemeine Hochschulreife
  • Biologie
  • 10
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Sometimes even enzymes are sated and have enough!

Need no more!
1
Match the fitting words and phrases.
auf einer Achse auftragen
1x
Bindungsstreben
1x
Geschwindigkeit
1x
sich trennen
1x
steigern
1x
Sättigung
1x
umsetzen
1x
  • saturation
  • to plot against
  • affinity
  • to convert
  • to enhance
  • velocity
  • to dissociate
2
Below you find sentences describing a specific moment in enzyme activity which is also termed reaction rate. Put the sentences into the correct order.
(1-6)
  • 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.
Michaelis Menten curve - the reaction rate of an enzyme depends on the substrate concentration, the number of enzymes stays constant
3
Match the texts with a suitable point in the graph.

(   ) 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.