Biochemistry
Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
Question
Book Icon
Chapter 8, Problem 26P
Interpretation Introduction

(a)

Interpretation:

The rearrangement of the Michaelis-Menten equationfor obtaining the V0 as a function of V0/[S] needs to be determined.

Concept introduction:

The Michaelis-Menten equation relates the concentration of substrate with the velocity of the reaction. A constant which expresses the substrate’s concentration if the velocity of reaction equals to the half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by KM.

Interpretation Introduction

(b)

Interpretation:

The significance of the slope, the y-intercept, and the x -intercept in a plot of V0 versus V0/[S] needs to be explained.

Concept introduction:

The Michaelis-Menten equation relates the concentration of substrate with the velocity of the reaction. A constant which expresses the substrate’s concentration if the velocity of reaction equals to the half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by KM.

Interpretation Introduction

(c)

Interpretation:

The graph between V0 and V0/[S] in inhibitor’s absence, in the presence of a competitive inhibitor and noncompetitive inhibitor needs to be plotted.

Concept introduction:

A molecule that disturbs or inhibits the activity of an enzyme is known as enzyme inhibitor. The enzyme inhibition stops the generation of enzyme-substrate complex which, in turn, inhibits the formation of the product. The three main types of inhibition are competitive inhibition, uncompetitive inhibition and noncompetitive inhibition.

Blurred answer
Students have asked these similar questions
The preferred substrate is T because the enzyme half-saturates at 7.00 mM for T, but requires 28.0 mM for U, and 112 mM for S. b Question Content Area The rate constant k 2 with substrate S is 9.60×107 sec-1, with substrate T, k 2 = 6.00×104 sec-1, and with substrate U, k 2 = 2.40×106 sec-1. Calculate the catalytic efficiency with S, T, and U. Catalytic efficiency with S =  Catalytic efficiency with T =   Catalytic efficiency with U =   Does enzyme A use substrate S, substrate T, or substrate U with greater catalytic efficiency?
Fumerase catalyzes the conversion of fumerate to malate. fumerate + H2O ⇋ malate The turnover number, kcat, for fumerase is 8.00×102 sec-1. The Km of this enzyme for fumerate is 5.00×10-3 μmol mL-1.   a   In an experiment using 2.00×10-3 μmol·mL-1, what is Vmax?
Suppose you wanted to make a buffer of exactly pH 7.00 using KH2PO4 and Na2HPO4. If the final solution was 0.18 M in KH2PO4, you would need 0.25 M Na2HPO4. Now assume you wish to make a buffer at the same pH, using the same substances, but want the total phosphate molarity ([HPO42−]+[H2PO−4]) to equal 0.20 M. What concentration of the Na2HPO4 would be required?
Knowledge Booster
Background pattern image
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
  • Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305577206
    Author:Reginald H. Garrett, Charles M. Grisham
    Publisher:Cengage Learning
    Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305961135
    Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
    Publisher:Cengage Learning
    Text book image
    Principles Of Pharmacology Med Assist
    Biology
    ISBN:9781337512442
    Author:RICE
    Publisher:Cengage
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Text book image
Principles Of Pharmacology Med Assist
Biology
ISBN:9781337512442
Author:RICE
Publisher:Cengage