Question

What are some defining characteristics of enzymes that obey Michaelis-Menten kinetics?

What are some defining characteristics of enzymes that obey Michaelis-Menten kinetics?

Science   Chemistry   
0 0
Add a commentTranscribed image text
Next >

Homework Answers

Answer #1

Allosteric enzymes obey Michaelis Menten kinetics.

The Michaelis-Menten model cannot account for the kinetic properties of many enzymes.
Allosteric enzymes  do not obey Michaelis-Menten kinetics .
These enzymes consist of multiple subunits and multiple active sites.
With allosteric catalysts, the catalytic activity influencing one substrate can change the properties of other dynamic destinations situated inside a similar compound.


The after effect of this connection harmony is an agreeable impact, which means the authoritative of the substrate to a chemical's dynamic site influences the official of substrate to other active sites..
This property of cooperativity records for the sigmodial bend of V0 versus the grouping of substrate.

0 0
Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Log In

Sign Up

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...
When analyses enzyme-kinetics, what can we know with Michaelis-Menten equation? Write down everything you can.
When analyses enzyme-kinetics, what can we know with Michaelis-Menten equation? Write down everything you can.
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...
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 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]
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...
For some transformation having kinetics that obey the Avrami equation (Equation 11.17), the parameter n is...
For some transformation having kinetics that obey the Avrami equation (Equation 11.17), the parameter n is known to have a value of 1.7. If, after 125 s, the reaction is 50% complete, how long (total time) will it take the transformation to go to 86% completion?
In the Michaelis-Menten mechanism, under what conditions will the rate law be at a maximum? A.k2[E]0...
In the Michaelis-Menten mechanism, under what conditions will the rate law be at a maximum? A.k2[E]0 << Km B.k2[E]0 >> Km C.[S]0 >> Km D.[S]0 << Km
Reptiles – are first amniotes. Why significant? What are some of their defining characteristics? Endothermic vs....
Reptiles – are first amniotes. Why significant? What are some of their defining characteristics? Endothermic vs. Exothermic.
ADVERTISEMENT
Need Online Homework Help?

Get Answers For Free
Most questions answered within 1 hours.

Ask a Question
ADVERTISEMENT