Question

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]

Answer 1

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