> See also:
> - [[Enzymes]]
> - [[Binding Curves and Hill Plots]]
> - [[Reaction Kinetics]]
> - [[Chemical Equilibria]]
# Enzyme Kinetics
Some enzymes
$E+S \xleftrightharpoons[k_{-1}]{k_1}ES\xrightarrow{k_2}P+E$
There is always a way to determine the initial concentrations:
- $[E]_o=[E]_t+[ES]_t$
- $[S]_o=[S]_t+[ES]_t$
## Slope/Rate of Reactions
> See also: [[Differentiation|Differentiation]]
The reaction velocity:
$v=\frac{d[P]}{dt}=k_2[ES]_t$
- In layman’s terms, the velocity (rate) of the reaction at any given time ($t$) is equal to the rate constant
---
**The Turnover Number**
$K_{\text{cat}}$
Number of substrate molecules converted into product per active site per second
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Rate Enhancement is a ratio of the rates of the catalyze and uncatalyzed reactions
## Michaelis-Menten Equation
Despite this diversity, *all enzymes can be analyzed such that their reaction rate/overall efficiency can be quantified.* To do this, we use the **Michaelis-Menten Equation**:
$v_o=\frac{v_{\max}[S]_o}{[S]_o+K_M}$
### Assump The Lump (waaa^2)
There are several assumptions that must be made before we can utilize the
### Assumption of Steady State
The Michaelis-Menten Equation assumes that the enzyme-substrate (ES) complex maintains a **steady state**
- Not to be confused with the *standard state* (of [[chemical thermodynamics]])
![[Pasted image 20231121132535.png|300]]
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Assumes that as soon as the reaction begins, *the rate at which the enzyme-substrate complex is consumed is equal to the rate at which it is formed*.
$\frac{d[ES]}{dt}=k_1[E]_t[S]_t-k_{-1}[ES]_t-k_2[ES]_t$
This equations lets us determine the concentration of the enzyme-substrate complex at any given time by considering the rate laws for its formation and breakdown.
Instead of all the junk above, we set it equal to 0:
$\frac{d[ES]}{dt}=0$
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**Assumption of Equilibrium**
The physiologically common condition that substrate is *in great excess* over enzyme ($[S] \gg [E]$)
ES maintains a steady state and $[ES]$ and
$K_M=\frac{k_{-1}+k_2}{k_1}$
> [!warning] **What About Non-Steady States?**
> While we assume that
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My initial thoughts on this content are: “how is this equation even useful if we have to make so many assumptions about the conditions”
I can see how it could be useful in experimental setups but can’t even begin to imagine how you would translate that information into a biological system while maintiaing any level of accuracy
### Effects of Inhibitors
## Lineweaver-Burk Plots