IV) Many enzymes obey simple Michaelis-Menten kinetics, which are summarized by the equation: rate = (V...

IV) Many enzymes obey simple Michaelis-Menten kinetics, which are summarized
by the equation:
rate = (V max [S])/([S]+K m ); where V max = maximum velocity, [S] = concentration
of substrate; and K m = the Michaelis constant.
It is instructive to plug in a few values of [S] into the equation to see how rate is
affected. What are the rates for [S] equal to zero, equal to K m , and equal to infinite
concentration? Show all work.

Solutions

Expert Solution

queen_honey_blossom answered 1 week ago

Next > < Previous

Related Solutions

For enzymes that follow Michaelis–Menten kinetics, the inhibitors that inhibit enzyme activity include reversible inhibitor and...

For enzymes that follow Michaelis–Menten kinetics, the inhibitors that inhibit enzyme activity include reversible inhibitor and irreversible inhibitor. 1. Describe the type of reversible inhibitor. 2. Suggest ways to distinguish between types of inhibitors through enzyme reaction experiments.

Initial rate data for an enzyme that obeys Michaelis-Menten kinetics are shown in the following table....

Initial rate data for an enzyme that obeys Michaelis-Menten kinetics are shown in the following table. When the enzyme concentration is 3 nmol ml−1, a Lineweaver-Burk plot of this data gives a line with a y-intercept of 0.00426 (μmol−1ml s). [S] μM v0 (μmol ml−1 s−1) 320 169 160 132 80.0 92.0 40.0 57.2 20.0 32.6 10.0 17.5 a. Calculate Kcat for the reaction b. Calculate Km for the enzyme cWhen the reactions in part (B) are repeated in the...

Derive the kinetic equations (Michaelis-Menten equation) about 3 reversible inhibition kinetics: competitive inhibition, uncompetitive equation, and...

Derive the kinetic equations (Michaelis-Menten equation) about 3 reversible inhibition kinetics: competitive inhibition, uncompetitive equation, and noncompetitive equation.

In Michaelis-Menten kinetics, what values would make an enzyme “good” at catalysis?

Provide specific example for allosteric enzymes. Do allosteric enzymes follow Michaelis-Menten? Explain

What are the key differences between the Michaelis-Menten model that describes enzyme kinetics and the Monod...

What are the key differences between the Michaelis-Menten model that describes enzyme kinetics and the Monod model that describes whole-cell or community kinetics?

Draw a Michaelis Menten graph to represent normal pyruvate carboxylase kinetics in the conversion of pyruvate...

Draw a Michaelis Menten graph to represent normal pyruvate carboxylase kinetics in the conversion of pyruvate to oxaloacetate. Explain why you drew things as you did.

Explain the meaning of the three assumptions for the Michaelis-Menten kinetics. Express each assumption in mathematical...

Explain the meaning of the three assumptions for the Michaelis-Menten kinetics. Express each assumption in mathematical terms.

When analyses enzyme-kinetics, what can we know with Michaelis-Menten equation? Write down everything you can.

A substrate is decomposed in the presence of an enzyme according to the Michaelis-Menten equation with...

A substrate is decomposed in the presence of an enzyme according to the Michaelis-Menten equation with the following kinetic parameters: Km = 20 g/L Vmax = 12.0 g/L-min (a) Determine the concentration of substrate after leaving the second reactor in a two-reactor series of 20-liter CSTRs. The flow rate is 2.00 L/min. The inlet substrate concentration is 40 g/L. The enzyme concentration in the two reactors is maintained at the same value all of the time. (b) Determine the conversion...

Subjects