Question

Enzyme Kinetics Please explain reasoning for answers. How does the [S] affect the rate of an...

Enzyme Kinetics Please explain reasoning for answers.

How does the [S] affect the rate of an enzymatic reaction? Why don’t enzyme catalyzed rates increase linearly with [S]?

How will Km (Michaelis Constant) it affect the rate of an enzymatic reaction? What will it change on the hyperbolic curve? Why is the kcat/Km ratio a superior way to compare one enzyme to another as compared to either of the two constants alone?

What happens to the Michaelis-Menten equation when [S] << Km? When [S] >> Km and when [S] = Km?

Homework Answers

Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for?
Ask your own homework help question
Similar Questions
An enzyme follows Michaelis-Menten kinetics. How does the following things affect the Km and the Vmax....
An enzyme follows Michaelis-Menten kinetics. How does the following things affect the Km and the Vmax. Explain how they are affected and why. 1. A competitive inhibitor 2. A Mixed inhibitor 3. 6 M urea 4. doubling [S]
In a particular enzyme-catalyzed reaction, Vmax = 0.2 mol/sec and Km = 5 mM. Assume the...
In a particular enzyme-catalyzed reaction, Vmax = 0.2 mol/sec and Km = 5 mM. Assume the enzyme shows standard Michaelis-Menten kinetics. What is the rate of the reaction when [S] = 10mM?
Which of the following in not true for an enzymatic reaction that shows Michaelis-Menten kinetics? Group...
Which of the following in not true for an enzymatic reaction that shows Michaelis-Menten kinetics? Group of answer choices the rate steadily decreases over the course of the reaction Vmax depends on the concentration of the enzyme in the presence of an inhibitor the v vs. [S] plot is a hyperbola the equilibrium constant is lower as compared to the uncatalyzed reaction KM is determined by finding the [S] at which v = Vmax/2
For any enzyme that follows simple Michaelis-Menten kinetics, when the initial velocity of the reaction is...
For any enzyme that follows simple Michaelis-Menten kinetics, when the initial velocity of the reaction is 1/5 of Vmax what is the Substrate concentration? A) KM << [S] B) KM = 1/5[S] C) KM = 4[S] D) KM = 5[S] E) KM = [S]
The following parameter(s) of an enzyme-catalyzed reaction depend(s) on enzyme concentration: A) Km (Michaelis constant) B)...
The following parameter(s) of an enzyme-catalyzed reaction depend(s) on enzyme concentration: A) Km (Michaelis constant) B) Vmax (maximum velocity) C) kcat (turnover number) D) A and B E) B and C Km is the equivalent of: A) Substrate concentration at Vo B) Substrate concentration when Vmax is reached C) Substrate concentration when 1/2 Vmax is reached D) Product concentration when 1/2 Vmax is reached
The zero order rate is seen in an enzyme catalyzed reaction when: A. There is too...
The zero order rate is seen in an enzyme catalyzed reaction when: A. There is too much enzyme and too little substrate B. Enzyme reactions are always first order C. The Michaelis constant is very high D. The Vmax of the reaction is twice that which is observed E. The enzyme substrate comples is at its maximum concentration What happens when you add more enzyme to a catalyzed reaction that already is proceeding at Vmax? A. The reaction is inhibited...
Experiment IV: Effect of pH on the Rate of Enzyme Reaction 1. How does pH affect...
Experiment IV: Effect of pH on the Rate of Enzyme Reaction 1. How does pH affect the rate of chemical reaction catalyzed by an enzyme?
The following rate constants were determined for a Michaelis-type enzyme: k1 = 2.5 x 10^9 M-1...
The following rate constants were determined for a Michaelis-type enzyme: k1 = 2.5 x 10^9 M-1 s -1 , k-1 = 5.0 x 10^3 s -1 , and k2 = 5.0 x 10^4 s -1 . a. What are the values of Km, Ks, and kcat for this enzyme? Is this a rapid equilibrium enzyme or does it just follow steady state kinetics? Explain the basis for your answer. b. What substrate concentration is needed to achieve half maximal velocity?...
Enzyme E, which follows Michaelis- Menten kinetics, catalyzes the same reaction upon three different substates that...
Enzyme E, which follows Michaelis- Menten kinetics, catalyzes the same reaction upon three different substates that are strucurally related (S1,S2, and S3) When the kinetic data for the three reactions are determined under the same reaction conditions, the data indicated below is otabined. The Km (Km1) for E and S1 is 1uM, that for E and S2 (Km2) is 80nM, and that for E and S3 (Km3) is 20nM. The Vmax for E and S1 is 115uMol/min (vmax1), Vmax2 is...
1. How does changing the temperature affect the rate of enzyme activity? 2. Why might the...
1. How does changing the temperature affect the rate of enzyme activity? 2. Why might the enzyme activity decrease at very high temperatures? 3. How does changing the concentration of substrate affect the rate of decomposition of H2O2 by catalase? 4. How does changing the PH affect the rate of enzyme activity?
ADVERTISEMENT
Need Online Homework Help?

Get Answers For Free
Most questions answered within 1 hours.

Ask a Question
ADVERTISEMENT