Question

Vmax and Km of an enzyme are 25mM/s and 5mM, respectively. What is initial velocity when...

Vmax and Km of an enzyme are 25mM/s and 5mM, respectively. What is initial velocity when substrate concentration is 10mM? Show work and include proper unit.
10nM of enzyme was used in the above question. Based on the kinetic parameters, has the enzyme achieved catalytic perfection? Show work. Thank you!

Homework Answers

Answer #1

Q1. Initial velocity is 1.67mM/s.

Q2. The enzyme has achieved catalytic perfection.

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
Vmax and Km of an enzyme are 25mM/s and 5mM, respectively. What is initial velocity when...
Vmax and Km of an enzyme are 25mM/s and 5mM, respectively. What is initial velocity when substrate concentration is 10mM? Show work and include proper unit. 10nM of enzyme was used in the above question. Based on the kinetic parameters, has the enzyme achieved catalytic perfection? Show work. Thank you!
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...
What is Vmax? a) The concentration of S at which the enzyme becomes saturated. b) The...
What is Vmax? a) The concentration of S at which the enzyme becomes saturated. b) The velocity at which enzyme E is saturated with substrate S. c) The initial velocity of the enzyme at v=[S]. d) One half of the limiting enzymatic rate.
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]
An enzyme catalyzes a reaction with an initial velocity of 50 micromoles/litre-seconds when the substrate concentration...
An enzyme catalyzes a reaction with an initial velocity of 50 micromoles/litre-seconds when the substrate concentration is 5 micromolar and 80 micromoles/litre-seconds when the substrate concentration is 10 micromolar. The Vmax and Km of this enzyme are: A) 50 micromoles/litre-seconds; 5 micromolar B) 80 micromoles/litre-seconds; 10 micromolar. C) 200 micromoles/litre-seconds; 15 micromolar D) 100 micromoles/litre-seconds; 12.5 micromolar E) 10 micromoles/litre-seconds; 1 micromolar
9. A.  Vmax is a poor metric for indicating enzyme efficiency because: 1) It changes as a...
9. A.  Vmax is a poor metric for indicating enzyme efficiency because: 1) It changes as a result of using competitive inhibitor 2) The total enzyme concentration affects the value of Vmax 3) It requires measuring enzyme velocity 4) It is independent of the total enzyme concentration 5) It varies as a function of the KM value of the substrate B. What is the main disadvantage of using kcat to compare the efficiencies of enzymes? What is the main advantage of...
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 data were obtained for the variation of initial velocity and substrate for a reaction...
The following data were obtained for the variation of initial velocity and substrate for a reaction catalyzed by chymotrypsin (5nM) at pH 8, 37 °C. 1. Using a linear plot, determine the KM and Vmax of the chymotrypsin given the data below: (12) [S] (μM) V0 (μmol/min) 0    0 0.5 200 1.0    400 1.5    580 2.0    750 2.5    840 3.0    860 4.0    875 6.0    890 The kcat/KM parameter is a measure of...
A biochemist obtains the following set of data for a mouse enzyme that is known to...
A biochemist obtains the following set of data for a mouse enzyme that is known to follow Michaelis- Menten kinetics. The experimental conditions were with 0.1 μmol of enzyme and pH 6.0. Substrate Initial concentration velocity (μM) (μmol/min) and Initial velocity 1 49 2 96 8 349 50 621 100 676 1,000 698 5,000 699 Question 1. Estimate what would be the initial velocity in μmol/min at a substrate concentration of 10,000 μM. Question 2. What is the approximate Vmax...