Concept:
The
Michaelis–Menten equation describes the relationship between the rate of an enzyme-catalyzed reaction and the concentration of substrate. It is expressed as:
\[
v = \frac{V_{max}[S]}{K_m + [S]}
\]
where:
- $v$ = reaction velocity
- $V_{max}$ = maximum reaction velocity
- $[S]$ = substrate concentration
- $K_m$ = Michaelis constant
Step 1:Understanding the meaning of $K_m$.
The constant $K_m$ represents the substrate concentration at which the reaction rate reaches
half of its maximum velocity ($V_{max}/2$).
Step 2:Interpreting enzyme affinity.
The value of $K_m$ also provides information about the
affinity of an enzyme for its substrate:
- Low $K_m$ value → High affinity (enzyme binds substrate easily)
- High $K_m$ value → Low affinity (enzyme binds substrate less efficiently)
Step 3:Selecting the correct option.
Since $K_m$ indicates the substrate concentration at which the reaction rate is half of $V_{max}$, option (B) is correct.
Conclusion:
Thus, the Michaelis constant $K_m$ represents the
substrate concentration required to reach half of the maximum reaction velocity.