Is the Uptake Equation Different When $k_2 = 0$?

  • MHB
  • Thread starter Dustinsfl
  • Start date
In summary, The Michaelis-Menten uptake is just the Michaelis constant and the differential equation model can be non-dimensionalized to a model with three equations and three initial conditions.
  • #1
Dustinsfl
2,281
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The question I have is: when $k_2 = 0$ sketch the uptake $r(u)$ as a function of $u$ and compare it with the Michaelis-Menten uptake.
If $k_2 = 0$, wouldn't that change everything significantly? Does that mean re-do everything with $k_2 = 0$.
Is the Michaelis-Menten uptake just Michaelis constant?$$
S + E \underset{k_{-1}}{\overset{k_1}{\rightleftharpoons}} C_1 \xrightarrow{k_2} E + P,
$$
$$
S + C_1 \underset{k_{-3}}{\overset{k_3}{\rightleftharpoons}} C_2\xrightarrow{k_4} C_1 + P
$$
Let $s = $, $e = [E]$, $c_1 = C_1$, $c_2 = [C_2]$, and $p = [P]$.
Then by the Law of Mass action, we can write down the differential equation model as:
\begin{align}
\frac{ds}{dt} =& -k_1es + (k_{-1} - k_3s)c_1 + k_{-3}c_2,\\
\frac{dc_1}{dt} =& k_1se - (k_{-1} + k_2 + k_3s)c_1 + (k_{-3} + k_4)c_2,\\
\frac{dc_2}{dt} =& k_3sc_1 - (k_{-3} + k_4)c_2,\\
\frac{de}{dt} =& -k_1se + (k_{-1} + k_2)c_1,\\
\frac{dp}{dt} =& k_2c_2 + k_4c_2
\end{align}
The initial conditions for the differential equation model are
$$
s(0) = s_0,\quad e(0) = e_0,\quad c_1(0) = c_2(0) = p(0) = 0.
$$
Since the enzyme is the catalyst, the enzyme is conserved by adding equations 2, 3, and 4.
$$
\frac{de}{dt} + \frac{dc_1}{dt} + \frac{dc_2}{dt} = 0\Rightarrow e(t) + c_1(t) + c_2(t) = e_0
$$
Then $e(t) = e_0 - c_1(t) - c_2(t)$.
Since $dp/dt$ is uncoupled, we can directly solve for $p(t)$.
$$
\int dp = \int (k_2c_1 + k_4c_2)dt\Rightarrow p(t) = k_2\int c_1dt + k_4\int c_2dt
$$
The only equations left to solve for are equations 1, 2, and 3 which are
\begin{align}
\frac{ds}{dt} =& -k_1e_0s + (k_{-1} + k_1s - k_3s)c_1 + (k_1s + k_{-3})c_2,\notag\\
\frac{dc_1}{dt} =& k_1e_0s - (k_{-1} + k_2 +k_1s +k_3s)c_1 + (k_{-3} + k_4 - k_1s)c_2,\notag\\
\frac{dc_2}{dt} =& k_3sc_1 - (k_{-3} + k_4)c_2,\notag
\end{align}
after substituting $e(t) = e_0 - c_1(t) - c_2(t)$.
By making the substitutions
\begin{alignat*}{4}
\tau &= k_1e_0t, & u &= \frac{s}{s_0}, & v_1 &= \frac{c_1}{e_0}, & v_2 &= \frac{c_2}{e_0},\notag\\
a_1 &= \frac{k_{-1}}{k_1s_0}, &\quad a_2 &= \frac{k_2}{k_1s_0}, &\quad a_3 &= \frac{k_3}{k_1}, &\quad a_4 &= \frac{k_{-3}}{k_1s_0},\notag\\
a_5 &= \frac{k_4}{k_1s_0}, & \epsilon &= \frac{e_0}{s_0}
\end{alignat*}
we can non-dimensionalize then model as
\begin{align}
\frac{du}{d\tau} =& -u + (u -a_3u + a_1)v_1 + (a_4 + u)v_2 = f(u,v_1,v_2),\notag\\
\epsilon\frac{dv_1}{d\tau} =& u - (u + a_3u + a_1 + a_2)v_1 +(a_4 + a_5 - u)v_2 = g_1(u,v_1,v_2),\notag\\
\epsilon\frac{dv_2}{d\tau} =& a_3uv_1 - (a_4 + a_5)v_2 = g_2(u,v_1,v_2).\notag
\end{align}
The initial conditions for the dimensionless model are
$$
u(0) = 1,\quad v_1(0) = v_2(0) = 0.
$$
Just as in class this model is a single perturbation for $0 < \epsilon\ll 1$.
Solving for $v_1$ and $v_2$, we obtain
$$
v_1 = \frac{u}{a_1 + a_2 + u + a_3u^2(a_4 + a_5)^{-1}} \quad\text{and}\quad v_2 = \frac{a_3uv_1}{a_4 + a_5}.
$$
Then
$$
f(u,v_1(u),v_2(u)) = \frac{du}{d\tau} = -u\frac{a_2 + a_3a_5u(a_4 + a_5)^-1}{a_1 + a_2 + u + a_3u^2(a_4 + a_5)^{-1}} = -r(u)
$$
is the uptake equation for $u$.
Let$A = a_2$, $B = a_3a_5(a_4 + a_5)^{-1}$, $C = a_1 + a_2$, and $D = a_3(a_4 + a_5)^{-1}$.
Then
$$
\frac{du}{d\tau} = -r(u) = -u\frac{A + Bu}{C + u + Du^2}.
$$
 
Last edited:
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  • #2
Would it be a simply substitution or would the non-dimensionalization have to be re-worked?

$$
S + E \underset{k_{-1}}{\overset{k_1}{\rightleftharpoons}} C_1,
$$
$$
S + C_1 \underset{k_{-3}}{\overset{k_3}{\rightleftharpoons}} C_2\xrightarrow{k_4} C_1 + P
$$
Let $s = $, $e = [E]$, $c_1 = C_1$, $c_2 = [C_2]$, and $p = [P]$.
Then by the Law of Mass action, we can write down the differential equation model as:
\begin{align}
\frac{ds}{dt} =& -k_1es + (k_{-1} - k_3s)c_1 + k_{-3}c_2,\\
\frac{dc_1}{dt} =& k_1se - (k_{-1} + 0 + k_3s)c_1 + (k_{-3} + k_4)c_2,\\
\frac{dc_2}{dt} =& k_3sc_1 - (k_{-3} + k_4)c_2,\\
\frac{de}{dt} =& -k_1se + (k_{-1} + 0)c_1,\\
\frac{dp}{dt} =& 0 + k_4c_2
\end{align}
The initial conditions for the differential equation model are
$$
s(0) = s_0,\quad e(0) = e_0,\quad c_1(0) = c_2(0) = p(0) = 0.
$$
Since the enzyme is the catalyst, the enzyme is conserved by adding equations 2, 3, and 4.
$$
\frac{de}{dt} + \frac{dc_1}{dt} + \frac{dc_2}{dt} = 0\Rightarrow e(t) + c_1(t) + c_2(t) = e_0
$$
Then $e(t) = e_0 - c_1(t) - c_2(t)$.
Since $dp/dt$ is uncoupled, we can directly solve for $p(t)$.
$$
\int dp = \int (0 + k_4c_2)dt\Rightarrow p(t) = 0 + k_4\int c_2dt
$$
The only equations left to solve for are equations 1, 2, and 3 which are
\begin{align}
\frac{ds}{dt} =& -k_1e_0s + (k_{-1} + k_1s - k_3s)c_1 + (k_1s + k_{-3})c_2,\notag\\
\frac{dc_1}{dt} =& k_1e_0s - (k_{-1} + 0 +k_1s +k_3s)c_1 + (k_{-3} + k_4 - k_1s)c_2,\notag\\
\frac{dc_2}{dt} =& k_3sc_1 - (k_{-3} + k_4)c_2,\notag
\end{align}
after substituting $e(t) = e_0 - c_1(t) - c_2(t)$.
By making the substitutions
\begin{alignat*}{4}
\tau &= k_1e_0t, & u &= \frac{s}{s_0}, & v_1 &= \frac{c_1}{e_0}, & v_2 &= \frac{c_2}{e_0},\notag\\
a_1 &= \frac{k_{-1}}{k_1s_0}, &\quad a_2 &= \frac{0}{k_1s_0}=0, &\quad a_3 &= \frac{k_3}{k_1}, &\quad a_4 &= \frac{k_{-3}}{k_1s_0},\notag\\
a_5 &= \frac{k_4}{k_1s_0}, & \epsilon &= \frac{e_0}{s_0}
\end{alignat*}
we can non-dimensionalize then model as
\begin{align}
\frac{du}{d\tau} =& -u + (u -a_3u + a_1)v_1 + (a_4 + u)v_2 = f(u,v_1,v_2),\notag\\
\epsilon\frac{dv_1}{d\tau} =& u - (u + a_3u + a_1 + 0)v_1 +(a_4 + a_5 - u)v_2 = g_1(u,v_1,v_2),\notag\\
\epsilon\frac{dv_2}{d\tau} =& a_3uv_1 - (a_4 + a_5)v_2 = g_2(u,v_1,v_2).\notag
\end{align}
The initial conditions for the dimensionless model are
$$
u(0) = 1,\quad v_1(0) = v_2(0) = 0.
$$
Just as in class this model is a single perturbation for $0 < \epsilon\ll 1$.
Solving for $v_1$ and $v_2$, we obtain
$$
v_1 = \frac{u}{a_1 + 0 + u + a_3u^2(a_4 + a_5)^{-1}} \quad\text{and}\quad v_2 = \frac{a_3uv_1}{a_4 + a_5}.
$$
Then
$$
f(u,v_1(u),v_2(u)) = \frac{du}{d\tau} = -u\frac{0 + a_3a_5u(a_4 + a_5)^-1}{a_1 + 0 + u + a_3u^2(a_4 + a_5)^{-1}} = -r(u)
$$
is the uptake equation for $u$.
Let$A = a_2=0$, $B = a_3a_5(a_4 + a_5)^{-1}$, $C = a_1 + a_2$, and $D = a_3(a_4 + a_5)^{-1}$.
Then
$$
\frac{du}{d\tau} = -r(u) = -u\frac{Bu}{C + u + Du^2}.
$$
 
  • #3
Michaelis-Menten uptake

So the Michaelis-Menten rate of uptake is
$$
R_0 = \frac{Q_{s_0}}{K_m+s_0}
$$
where $K_m=\dfrac{k_{-1}+k_2}{k_1}$ and $Q_{s_0}=k_2e_0s_0$

Q is the max velocity K_m is the Michaelis constant.

How can I plot this in Mathematica?
 
  • #4
Re: Michaelis-Menten uptake

​Solved
 
  • #5

When $k_2 = 0$, $A = 0$, and
$$
r(u) = u\frac{Bu}{C + u + Du^2} = \frac{u^2}{\frac{C}{B} + \frac{u}{B} + u^2D}.
$$
The Michaelis-Menten uptake equation is
$$
r(u) = \frac{u}{u + \frac{1}{D}}.
$$
The Michaelis constant is $K_M = \frac{1}{D}$.
When $k_2 = 0$, the uptake equation is not linear and does not have a Michaelis constant.
 

FAQ: Is the Uptake Equation Different When $k_2 = 0$?

What is an allosteric enzyme?

An allosteric enzyme is a type of enzyme that can change its shape and activity in response to the binding of a molecule to a site on the enzyme that is not the active site. This binding can either activate or inhibit the enzyme's activity.

How does allosteric regulation work?

Allosteric regulation works by the binding of a molecule, called an allosteric effector, to a specific site on the enzyme, called an allosteric site. This binding causes a conformational change in the enzyme, altering its activity and ability to bind to its substrate.

What are the advantages of allosteric enzymes?

Allosteric enzymes have several advantages over other types of enzymes. They can be regulated more quickly and efficiently, allowing for rapid responses to changes in the cell's environment. They also allow for fine-tuning of enzyme activity, providing more precise control over metabolic processes.

Can allosteric enzymes be inhibited?

Yes, allosteric enzymes can be inhibited by the binding of an allosteric inhibitor to the allosteric site. This causes a conformational change that decreases the enzyme's activity. Allosteric inhibition can be reversible or irreversible, depending on the strength of the inhibitor's binding to the enzyme.

How are allosteric enzymes different from other types of enzymes?

Allosteric enzymes differ from other types of enzymes in that they have an additional regulatory site, the allosteric site, which can affect the enzyme's activity. Other types of enzymes typically only have the active site where the substrate binds and the reaction takes place.

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