This is the answer key from the teacher and the highlighted parts are the correct answer for the question. I'm not sure how they got the numbers for [S] and km. Could you explain in detail how to do it?
This is the answer key from the teacher and the highlighted parts are the correct answer for the question. I'm not sure how they got the numbers for [S] and km. Could you explain in detail how to do it?
![If the \( K_m \) for an enzyme is \( 1 \times 10^{-5} \) M and the substrate concentration is \( 1 \times 10^{-6} \) M, what is \( V_0 \) in terms of \( V_{max} \) for the enzyme?
Given:
- \([S] = \frac{1}{10} K_m\)
- \([S] = 1, K_m = 10 \)
Calculation:
\[ V_0 = V_{max} \frac{1}{(1) + (10)} = \frac{V_{max}}{11} \]](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fd824104a-96bc-4561-8672-0656666c77c0%2F0d5c2a34-974e-4177-8be8-51d565edffb2%2Fta18fio_processed.png&w=3840&q=75)
Enzymology relies on the fundamental idea of Michaelis-Menten kinetics. It covers the interactions between substrates and enzymes that catalyze reactions.
According to this concept, the connection between substrate concentration and reaction rate is hyperbolic as well as incorporates the development of an enzyme-substrate complex. This relationship is quantified by the Michaelis-Menten equation, where Km stands for the substrate concentration whereby the reaction rate is half that of the maximal rate (Vmax).
In biochemistry and pharmacology, this model is frequently used to better explain the behavior of enzymes.
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