The Michaelis‑Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V 0 V0 for an enzyme‑
catalyzed, single‑substrate reaction E + S − ⇀ ↽ − ES ⟶ E + P E+S↽−−⇀ES⟶E+P . The model can be more readily understood when comparing three conditions:
[ S ] < [ S ]>>Km
[ S ] = K m
Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V 0 where steady state conditions are assumed. [ E total ] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme.
1. [ S ] < 2. [ S ]>>Km
3. [ S ] = K m
4. Not true for any of these conditions.
A. [Efree] is about equal to [Etotal]
B. Half of the active sites are filled with S.
C. [ES] is much lower than [Efree]
D. Almost all active sites will be filled.
E. Increasing [Etotal] will lower Km.
F. Reaction rate is independent of [S]
[ S ] < [ S ]>>Km
[ S ] = K m
Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V 0 where steady state conditions are assumed. [ E total ] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme.
1. [ S ] < 2. [ S ]>>Km
3. [ S ] = K m
4. Not true for any of these conditions.
A. [Efree] is about equal to [Etotal]
B. Half of the active sites are filled with S.
C. [ES] is much lower than [Efree]
D. Almost all active sites will be filled.
E. Increasing [Etotal] will lower Km.
F. Reaction rate is independent of [S]
1 answer:
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Answer:
The Michaelis‑Menten equation is given as
v₀ = Kcat X [E₀] X [S] / (Km + [S])
where,
Kcat is the experimental rate constant of the reaction; [s] is the substrate concentration and
Km is the Michaelis‑Menten constant.
Explanation:
See attached image for a detailed explanation
