Draw a double reciprocal plot for a typical Michaelis Menton enzyme and an allosteric enzyme that...

Draw a double reciprocal plot for a typical Michaelis Menton enzyme and an allosteric enzyme that has the same Vmax and Km value. Also raw a double reciprocal plot for for the allosteric enzyme in the absence and presence of the allosteric inhibitor.

Expert Solution

(please up vote thank you....)

gladiator answered 1 year ago

biochem: Derive the Michaelis–Menten kinetics and note the important assumptions. Also indicate why a double reciprocal...

biochem: Derive the Michaelis–Menten kinetics and note the important assumptions. Also indicate why a double reciprocal plot is linear.

Sketch a general Lineweaver-Burke plot that illustrates the kinetic behavior of a non-allosteric enzyme. Identify on...

Sketch a general Lineweaver-Burke plot that illustrates the kinetic behavior of a non-allosteric enzyme. Identify on your plot the features that allow one to determine Vmax and KM for the enzyme. How would one use a Lineweaver-Burke plat of enzyme kinetic data to identify an inhibitor's mode of action?

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

What makes phosphofructokinase the key allosteric enzyme in glycolysis?

Describe allosteric regulation of enzyme activity. How does allosteric inhibition differ from other modes of regulation,...

Describe allosteric regulation of enzyme activity. How does allosteric inhibition differ from other modes of regulation, and how can these work in concert to finely regulate enzyme activity? Provide an example, describe in detail, and use diagrams to help illustrate your point.

Describe the role of the bifunctional enzyme in the reciprocal regulation of glycolysis and gluconeogenesis.

Provide a detailed rationale for the observation that an enzyme that stabilizes its Michaelis (ES) complex...

Provide a detailed rationale for the observation that an enzyme that stabilizes its Michaelis (ES) complex as much as its transition state does not catalyze a reaction. Include appropriate reaction coordinate diagrams to support your answer.

In a 50µl reaction containing 0.25 pmol of a Michaelis enzyme with Km = 4.0 x...

In a 50µl reaction containing 0.25 pmol of a Michaelis enzyme with Km = 4.0 x 10-7 M and substrate concentration of 2 x 10-7 M, product was formed at an initial velocity of 5.0 x 10-5 Mmin-1 . a. If the enzyme concentration is doubled to 0.5 pmol in the reaction, how much will the velocity increase? Show mathematically

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

Describe how allosteric regulators may inhibit or stimulate the activity of an enzyme and how this...

Describe how allosteric regulators may inhibit or stimulate the activity of an enzyme and how this can be used by the cell to regulate metabolic pathways. (in paragraphs)

Question