What does a Michaelis-Menten graph show?
What does a Michaelis-Menten graph show?
Explanation: In a classic Michaelis-Menten graph, the y-axis represents reaction rate and the x-axis represents substrate concentration. At low substrate concentrations, the reaction rate increases sharply.
How do you graph a Michaelis-Menten plot?
Using graph paper, draw an x- and y-axis. Label the x-axis mM of [S] or concentration of substrate. Label the y ax- sec/micro-mole of V or velocity of reaction. Insert different values of [S] into the Michaelis-Menten equation, along with the values found for Km and Vmax, to solve for V.
How do you tell if an inhibitor is competitive or not?
Competitive and non-competitive inhibitors can be told apart by how they affect an enzyme’s activity at different substrate concentrations. If an inhibitor is competitive, it will decrease reaction rate when there’s not much substrate, but can be “out-competed” by lots of substrate.
What is the slope of a Michaelis-Menten plot?
The slope of the line is Km/Vmax, and the y-intercept is 1/Vmax. The x-intercept occurs at x = −1/Km.
How do you graph enzyme activity?
When plotting line graphs for enzyme rate experiments, remember the following:
- Plot data points accurately.
- Use appropriate linear scales on axes.
- Choose scales that enable all data points to be plotted within the graph area.
- Label axes, with units included.
- Make graphs that fill the space the exam paper gives you.
What happens to Km and Vmax in competitive inhibition?
In competitive inhibition, this doesn’t occur detectably, because at high substrate concentrations, there is essentially 100% of the enzyme active and the Vmax appears not to change. Additionally, KM for non-competitively inhibited reactions does not change from that of uninhibited reactions.
Why is the Michaelis-Menten graph hyperbolic?
This is because it takes a very small amount (i.e., low concentration) of the substrate to reach 50% of the saturating concentration. Conversely, a high numerical value of Km is indicative of a low affinity of the enzyme/transporter for its substrate.
Is Michaelis-Menten plot logarithmic?
A logarithmic method is described for the calculation of the transport parameters, Km and Vmax.’ of a biological system obeying Michaelis–Menten kinetics. 2. This logarithmic method leads to a way of estimating the transport parameters that has not apparently been used previously.
What is Km on a graph?
Km is the substrate concentration at which the initial reaction rate is equal to 1/2 Vmax. One way to avoid this type of confusion is to note that the units are completely different.