Question

Chemistry

Posted 3 months ago

```
The enzyme concentration $[t]=0.00012 \mathrm{mmol} / \mathrm{L}$
Use the information of substrate concentration [S] and rate $\mathrm{V}_{0}$ for both experiments, with inhibitor and without inhibitor to answer the following questions
\begin{tabular}{|c|c|c|}
\hline (NOTE: $[\mathbf{E}]=$ & Experiment 1 & Experiment 2 \\
\hline $\mathbf{0 . 0 0 0 1 2} \mathbf{~ m m o l} / \mathrm{L})$ & without inhibitor & with inhibitor \\
\hline & & {$[1]=0.033 \mathrm{mmol} / \mathrm{L}$} \\
\hline$[\mathrm{S}], \mathrm{mmol} / \mathrm{L}$ & $v 0, \mathrm{mmol} / \mathrm{L}-\mathrm{min}$ & $\mathrm{v} 0, \mathrm{mmol} / \mathrm{L}-\mathrm{min}$ \\
\hline 0.710 & 0.200 & 0.180 \\
\hline 0.400 & 0.180 & 0.150 \\
\hline 0.310 & 0.160 & 0.110 \\
\hline 0.098 & 0.120 & 0.070 \\
\hline 0.066 & 0.100 & 0.050 \\
\hline 0.040 & 0.070 & 0.040 \\
\hline
\end{tabular}
1- Calculate $\mathrm{Km}$ and Vmax for both experiments using Michaelis-Menten equation. [S] vs $\mathrm{V}_{0}$
2- Calculate $\mathrm{Km}$ and Vmax for both experiments using Lineweaver-Burk plot, 1 /[S] vs $1 / v_{0}$
3- Calculate Kcat for the enzyme (without inhibition)
4- Based on the values of $\mathrm{Km}$ and Vmax, with inhibitor and without inhibitor, determine the type of the Inhibition (competitive, non-competitive or uncompetitive)
```

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Answer from Sia

Posted 3 months ago

Solution

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3

Answer

$K_m$ and $V_{max}$ for both experiments would be estimated from the graph. The exact values would depend on the graph's accuracy.

Key Concept

Michaelis-Menten kinetics relate the rate of enzymatic reactions to substrate concentration.

Explanation

$V_{max}$ is the maximum reaction rate achieved by the system, at saturating substrate concentration, and $K_m$ is the substrate concentration at which the reaction rate is half of $V_{max}$.

Solution

1

2

3

Answer

$K_m$ and $V_{max}$ for both experiments would be calculated from the Lineweaver-Burk plot. The exact values would depend on the plot's accuracy.

Key Concept

Lineweaver-Burk plot is a double reciprocal graph used to determine enzyme kinetics.

Explanation

It linearizes the Michaelis-Menten equation, allowing for easier determination of $K_m$ and $V_{max}$ from the slope and y-intercept of the plot.

Solution

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Answer

$K_{cat}$ would be calculated using the $V_{max}$ from experiment 1 (without inhibitor) and the given enzyme concentration $[E]$.

Key Concept

$K_{cat}$ is the turnover number, representing the catalytic activity of an enzyme.

Explanation

It is calculated by dividing the maximum rate $V_{max}$ by the enzyme concentration $[E]$.

Solution

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Answer

The type of inhibition would be determined by comparing the changes in $K_m$ and $V_{max}$ for both experiments. The exact type would depend on the calculated values.

Key Concept

The type of enzyme inhibition can be determined by analyzing changes in $K_m$ and $V_{max}$.

Explanation

Competitive inhibitors increase $K_m$ without affecting $V_{max}$, non-competitive inhibitors decrease $V_{max}$ without affecting $K_m$, and uncompetitive inhibitors decrease both $K_m$ and $V_{max$ proportionally.

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