From the table in the image attached below, the row which is correct for an enzyme with a low Michaelis-Menten constant is: B. High; Low.
An enzyme can be defined as a biological catalyst (globular proteins) that typically speeds up or accelerates the rate of a chemical reaction by lowering the activation energy of its chemical reactants.
Michaelis–Menten kinetics is a commonly used model of enzyme kinetics and it describes the gross mechanism and velocity of an enzyme-catalyzed chemical reaction.
Also, it was named after Leonor Michaelis and Maud Menten.
Mathematically, the Michaelis–Menten kinetics is given by the formula:
[tex]v=\frac{V_{max} \;[S]}{K_M \;+ \;[S]}[/tex]
Where:
- v is the velocity of reaction.
- [S] is the concentration of a substrate (S).
- [tex]K_M[/tex] is the Michaelis-Menten constant.
[tex]V_{max}[/tex] is the maximum rate achieved.
Generally, an enzyme has a low Michaelis-Menten constant when the affinity of enzyme for substrate (S) is high and the substrate (S) concentration rate at maximum reaction rate ([tex]V_{max}[/tex]) is low.
In conclusion, only row B of the table in the image attached below satisfy this condition of enzyme with a low Michaelis-Menten constant.
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