How do you plot a Michaelis-Menten graph?

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.

What does Michaelis-Menten equation calculate?

The Michaelis-Menten equation calculator allows you to discover the kinetics of one-substrate reaction catalyzed with an enzyme. Michaelis-Menten kinetics allows you to calculate the rate of the reaction, V, substrate concentration, Km, and the maximum rate of reaction, Vmax.

What is the Lineweaver-Burk reaction?

The Lineweaver–Burk plot was widely used to determine important terms in enzyme kinetics, such as Km and Vmax, before the wide availability of powerful computers and non-linear regression software. The y-intercept of such a graph is equivalent to the inverse of Vmax; the x-intercept of the graph represents −1/Km.

Which of the following is true about Michaelis Menten equation?

Which of the following is true about Michaelis-Menten kinetics? Explanation: Km is defined as the concentration of substrate at which enzyme is working at half of maximum velocity. Explanation: At low substrate concentration, the rate of a reaction is determined by the rate of formation of an enzyme-substrate complex.

What is the Michaelis-Menten equation and its Lineweaver-Burk form?

The Lineweaver-Burk equation is a linear equation, where 1/V is a linear function of 1/[S] instead of V being a rational function of [S]. The Lineweaver-Burk equation can be readily represented graphically to determine the values of Km and Vmax. Given a Lineweaver-Burk plot, determine the Km of a particular enzyme.

What is the Michaelis Menten calculator?

Michaelis-Menten Equation Calculator. Michaelis menten equation is used for determining rates of enzyme controlled reactions. In the Michaelis-Menten equation v denotes the rate of the reaction, v max denotes the maximum rate that was achieved by the system, [S] denotes the Substrate concentration and K m denotes the Michaelis Constant.

What is the Michaelis-Menten equation for enzymes?

The Michaelis-Menten equation can be expressed as: The velocity is therefore proportional to the enzyme concentration , not inversely so. is also referred to as the turnover number. As the substrate concentration keeps increasing, then we end up with a steady state in which all the enzyme is bound.

What is the Michaelis mentenequation used for?

The Michaelis-Mentenequation (see below) is commonly used to study the kinetics of reaction catalysis by enzymes as well as the kinetics of transport by transporters. Typically, the rate of reaction (or reaction velocity) is experimentally measured at several substrate concentration values.

How do you find the Michaelis constant from Vmax?

The Michaelis constant (Km) is equal to the substrate concentration at which the reaction rate is half of vmax . It is often assumed that a biochemical reaction involving a single substrate would obey this equation. The Michaelis Menten equation can be derived using the steady state approximation.