Question

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]

Homework Answers

Answer #1

Correct option:     A) KM << [S]

V0 = Vmax ([S]/([S] + KM))

if initial concentration V0 = Vmax /5 then

KM = -1.25[S]

This represents KM << [S], this can be also obtained from Lineweaver-Burke plot.

Thank You So Much! Please Rate this answer as you wish.

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
1) For an enzyme that displays Michaelis-Menten kinetics, what is the initial velocity as a function...
1) For an enzyme that displays Michaelis-Menten kinetics, what is the initial velocity as a function of Vmax when: i) [S] = Km ii) [S] = 0.1 Km iii) [S] = 50Km 2) An enzyme (follows Michaelis-Mentin Kinetics) has Km = 0.5 M. The initial velocity is 0.2 Mmin-1 at substrate concentration of 50 M. What is the Vmax? What is the initial velocity when a) [S] = 2 M and b) [S] = 0.5 M? 3) What will be...
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]
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
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
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...
Michaelis-Menten kinetics define the way in which enzymes behave at various substrate concentrations. Unlike the linear...
Michaelis-Menten kinetics define the way in which enzymes behave at various substrate concentrations. Unlike the linear reaction rates discussed in organic chemistry, enzymes can only turn over substrate at a rate that is equal to or less than the amount of time it takes to bind to the enzyme, therefore, at high enough substrate concentrations, there will be no effect on the reaction rate. This is termed reaching Vmax, or the maximum velocity the enzyme can turn over product. From...
The Michaelis-Menten equation is an expression of the relationship between the initial velocity,V0, of an enzymatic...
The Michaelis-Menten equation is an expression of the relationship between the initial velocity,V0, of an enzymatic reaction and substrate concentration, [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation to an expression from which the effect of [S] on the rate can be more readily determined. Match the condition (e.g. [S] = Km) with the statement(s) that describe it: 1. Doubling [S] will almost double the rate. 2. Half of the active sites are occupied by...
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...
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?...
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?
ADVERTISEMENT
Need Online Homework Help?

Get Answers For Free
Most questions answered within 1 hours.

Ask a Question
ADVERTISEMENT