Question

The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations....

The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are as follows:

[S](μmol/L)   v[(μmol/L)min−1]

5   22

10   39

20    65

50   102

100   120

200   135.

a) Using Excel or any graphing software, create the Lineweaver-Burk plot and estimate Vmax.

b) Using the same Lineweaver-Burk plot that you created, estimate 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
For an enzyme-catalyzed reaction, the initial velocity was determined at two different concentrations of the substrate....
For an enzyme-catalyzed reaction, the initial velocity was determined at two different concentrations of the substrate. Which of the following would be closest to the value of Vmax? For an enzyme-catalyzed reaction, the initial velocity was determined at two different concentrations of the substrate. Which of the following would be closest to the value of Km? [S] (mM) Vo(mM/min) 1.0 2.0 4.0 2.8
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. 
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...
The kinetics of an enzyme were studied in the absence and presence of two different concentrations...
The kinetics of an enzyme were studied in the absence and presence of two different concentrations of an inhibitor. Determine the Km and Vmax of the uninhibited enzyme and identify which class of inhibitor is present using the data presented below. Use this data to determine the KI, the binding constant of the inhibitor to the enzyme. Note that this question will require you to use a computer-graphing program such as EXCEL.   [S] mmol/L vo (mmol/L)min-1 (no inhibitor) vo (mmol/L)min-1...
1) Spingospine 1-phosphate (SPP) has recently been discovered to be important for the cell survival. The...
1) Spingospine 1-phosphate (SPP) has recently been discovered to be important for the cell survival. The synthesis of SPP from Spingospine and ATP is catalyzed by the enzymes Spingospine kinase. An understanding of the kinetics of the Spingospine kinase reaction may be important in the development of drugs to treat cancer. The velocity of Spingospine kinase reaction was measured in the presence and absence of threospingospine, a stereoisomer of singspiel. The results are shown below. [Spingospine] (uM) Vo (umol/min) (No...
ADVERTISEMENT
Need Online Homework Help?

Get Answers For Free
Most questions answered within 1 hours.

Ask a Question
ADVERTISEMENT