Question

In an enzymatically catalyzed reaction, when most of an enzyme is in the form of the...

In an enzymatically catalyzed reaction, when most of an enzyme is in the form of the ES complex and the substrate is most likely to be turned into product, the observed rate will be defined by the value of Vmax regardless of how much the substrate concentration exceeds the level that is sufficient to maintain the enzyme in the form of the ES complex.

True or False?

Homework Answers

Answer #1

when the substrate concentration is high such that all the free enzymes are bound with the substrate ( all the enzymes are saturated with substrates) to form Enzyme substrate complex, then the substrate is converted to the product at the maximum rate, since all the enzymes are bound with the substrate the rate of reaction cannot be increased by increasing the concentration of the substrate and the rate of reaction at this point is called Vmax, so the given statement is true.

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
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 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
a) The Km of an enzyme of an enzyme-catalyzed reaction is 7.5 µM. What substrate concentration...
a) The Km of an enzyme of an enzyme-catalyzed reaction is 7.5 µM. What substrate concentration will be required to obtain 65% of Vmax for this enzyme? (same enzyme was used in part a and b) b) Calculate the Ki for a competitive inhibitor whose concentration is 7 x10-6 M. The Km in the presence of inhibitor was found to be 1.2x10-5 M. 
An enzyme-catalyzed reaction was carried out with the substrate concentration initially a thousand times greater than...
An enzyme-catalyzed reaction was carried out with the substrate concentration initially a thousand times greater than the Km for that substrate. After 9 minutes, 1% of the substrate had been converted to product, and the amount of product formed in the reaction mixture was 12 mmol. If, in a separate experiment, one-third as much enzyme and twice as much substrate had been combined, how long would it take for the same amount (12 mmol) of product to be formed?
An enzyme-catalyzed reaction was carried out with the substrate concentration initially 3500 times greater than the...
An enzyme-catalyzed reaction was carried out with the substrate concentration initially 3500 times greater than the Km for that substrate. After 9 minutes, 1% of the substrate had been converted to product, and the amount of product formed in the reaction mixture was 12 micro-moles. If, in a separate experiment, the same amount of substrate but six times as much enzyme had been combined in the same volume, how long would it take for the same amount (12 micro-moles) of...
An enzyme-catalyzed reaction was carried out with the substrate concentration initially two hundred times greater than...
An enzyme-catalyzed reaction was carried out with the substrate concentration initially two hundred times greater than the Km for that substrate. After 5 minutes, 1% of the substrate had been converted to product, and the amount of product formed in the reaction mixture was 30 micro mol. If, in a seperate experiment, TWO TIMES MORE enzyme and twice as much substrate had been combined, how long would it take for the same amount (30 micro mol) of product to be...
1.   Which of the following is true of enzyme catalyzed reactions? a.   Reaction rates are temperature dependent b.   Reaction...
1.   Which of the following is true of enzyme catalyzed reactions? a.   Reaction rates are temperature dependent b.   Reaction rates are pH dependent c.   Reaction rates depend on substrate concentration d.   Reaction rates depend on enzyme structure e.   All of the above f.    a, b, and c 2.   Which of the following is NOT true of enzymes? a.   Enzyme activity depends on reaction conditions. b.   Enzymes are catalysts that decrease the rate of reaction. c.   Enzymes can be inhibited by other proteins d.   Enzymes do not alter the change in free energy...
An enzyme-catalyzed reaction was carried out with the substrate concentration initially three hundred times greater than...
An enzyme-catalyzed reaction was carried out with the substrate concentration initially three hundred times greater than the Km for that substrate. After five minutes, 1% of the substrate had been converted to product, and the amount of product formed in the reaction mixture was 15 micro moles. If, in a seperate experiment, four times less enzyme and twice as much substrate had been combined, how long would it take for the same amount (15 micro moles) of product to be...
true or false question ____ The most common form of penicillin resistance occurs when bacteria evolve...
true or false question ____ The most common form of penicillin resistance occurs when bacteria evolve an enzyme that cleaves penicillin. ____ Glucose and galactose are 4-anomers of each other. ____ When a ketohexose cyclizes, carbon 2’s oxygen becomes the ring oxygen. Which statement is correct about the Michaelis-Menten constant, K​m,​ for the enzymatic reaction below? k​1​ k​2 E + S ​→​ ES ​→​ E + P A. It is numerically equal to the velocity that is one half the...
Please mark the following statements true or false. Correct the false statements using minimal changes. 1)...
Please mark the following statements true or false. Correct the false statements using minimal changes. 1) A transition state analogue enhances the activity of the enzyme when bound to it. 2. In the induced-fit model, the active site of the enzyme changes its conformation to fit the substrate and its transition state. 3. The Enzyme-Substrate complex must form before the enzyme-catalyzed reaction can take place. 4. Enzyme reduces the energy of the transition state, thus accelerate reaction.
ADVERTISEMENT
Need Online Homework Help?

Get Answers For Free
Most questions answered within 1 hours.

Ask a Question
ADVERTISEMENT