How do you read a Michaelis-Menten graph?

How do you read a Michaelis-Menten graph?

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.

Why does competitive inhibition increase Km value?

When the competitive inhibitor binds the enzyme, it is effectively ‘taken out of action. Why then, does Km appear higher in the presence of a competitive inhibitor. The reason is that the competitive inhibitor is reducing the amount of active enzyme at lower concentrations of substrate.

What is Km in the Michaelis Menten equation?

KM (the Michaelis constant; sometimes represented as KS instead) is the substrate concentration at which the reaction velocity is 50% of the Vmax. [S] is the concentration of the substrate S.

How do you calculate inhibition?

If X is the signal at a given concentration of inhibitor, calculate % inhibition with this equation: % inhibition = 100 x [1 – (X – MIN)/(MAX – MIN)].

What do Michaelis-Menten graphs and enzyme inhibition graphs show?

During the interviews, students were provided a Michaelis-Menten graph, a reaction scheme, and a graph depicting enzyme inhibition; these were used as an opportunity to investigate students’ reasoning related to enzyme kinetics.

What are Michaelis–Menten kinetics?

E.W.K. Young, in Modeling of Microscale Transport in Biological Processes, 2017 Michaelis–Menten kinetics were originally derived as a mathematical model of enzymatic reaction rates, and are frequently used to describe the uptake of nutrients like oxygen by cultured cells ( Cho et al., 2007 ).

Is there a mechanistic basis for the Michaelis–Menten equation?

The Michaelis–Menten equation has often been fitted to species accumulation data. It is a widely known function that has a finite asymptote, is nondecreasing, and accommodates a wide range of curvatures. The equation states that Soberón and Llorente (1993) use a birth chain model to suggest a mechanistic basis for the Michaelis–Menten equation.

Why does the curve of the Michaelis-Menten graph level off?

Why is it that as substrate concentration increases, the curve of the graph levels off and reaches a plateau? In a classic Michaelis-Menten graph, the y-axis represents reaction rate and the x-axis represents substrate concentration.