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188 - Biochemistry Physiology) Michaelis Menten Equation @hüning Q - A
188 - Biochemistry Physiology) Michaelis Menten Equation @hüning Q - A
QUESTIONS ANSWERS
1) What does the steady state assumption say? d) The rate of ES formation equals the rate of ES
a) The rate of ES formation equals the rate of product disassociation
formation
b) The rate of all reactions is equal
c) The rate of ES disassociation equals the rate of
product formation
d) The rate of ES formation equals the rate of ES
disassociation
3) When does 𝒌𝒌𝒎𝒎 have the same value as the substrate b) At half of maximal rate
concentration?
a) At maximal rate
b) At half of maximal rate
c) At the end
d) When the steady state assumption is met
4) What can a low 𝒌𝒌𝒎𝒎 tell us? c) The affinity of an enzyme to its substrate is high
a) The affinity of an enzyme to its substrate is low
b) The affinity of an enzyme to its substrate is always Example:
equal Hexokinase has a lower km than glucokinase.
c) The affinity of an enzyme to its substrate is high → Hexokinase has higher affinity to glucose than glucokinase
d) The affinity of an enzyme to its substrate is zero
5) What does a low substrate affinity mean? a) The enzyme can take larger amounts of substrate
a) The enzyme can take larger amounts of substrate
b) The enzyme can take lesser amounts of substrate
c) The enzyme is independent of ATP
d) All enzymes can take the same amount of substrate