SAPLINGPLUS FOR PRINCIPLES OF BIOCHEMIS
SAPLINGPLUS FOR PRINCIPLES OF BIOCHEMIS
7th Edition
ISBN: 9781319424572
Author: nelson
Publisher: MAC HIGHER
bartleby

Concept explainers

bartleby

Videos

Question
Book Icon
Chapter 6, Problem 8P

(a)

Summary Introduction

To determine: The substrate concentration at which an enzyme with a Kcat of 30.0s-1 and Km  of 0.0050M operate at one-quarter of its maximum rate.

Introduction:

Kcat is defined as a constant that is used to describe turnover rate of enzyme-substrate complex into product and enzyme. It is a turnover number of an enzyme which is used to indicate the conversion of maximum number of substrate into product per active site per unit time.

(a)

Expert Solution
Check Mark

Explanation of Solution

Explanation:

The formula for calculating concentration of substrate (V°)=Vmax[S]Km+[S] (1)

The values for Kcat, Km and V are substituted in the formula for calculating concentration of substrate,

V°=Vmax[S]Km+[S]0.25Vmax=Vmax[S]Km+[S]0.25=[S][Km]+[S]0.25[Km]+0.25[S]=[S]0.25[Km]=[S]0.25[S]0.25[Km]=0.75[S]0.25[Km]0.75=[S][S]=0.33[Km]=0.33×0.0050=0.00165=1.65×103M

Conclusion

Conclusion:

The concentration of substrate is 1.65×10-3M

(b)

Summary Introduction

To determine: The fraction of Vmax which is obtained at following substrate concentrations [S]=12Km,2Km ,and 10 Km.

Introduction:

Enzyme kinetics is defined as the study of chemical reactions which is catalyzed by enzyme. It indicates a rate of reaction as a function of substrate concentration with Vmax and Km of enzyme.

(b)

Expert Solution
Check Mark

Explanation of Solution

Explanation:

The formula for calculating fractions of Vmax at different substrate concentrations is,

V°=Vmax+[S][S] (Michaelis-Menten equation ) (2)

Substituting the value of  [S]=12Km

V°Vmax=[S]Km+[S]=12KmKm+12Km=12Km2+12Km=1232=0.51.5=0.33

Substituting the value of [S]=2Km in equation (2),

V°Vmax=[S]Km+[S]=2KmKm+2Km=23=0.66

Substituting the value of [S]=10Km in equation (2),

V°Vmax=[S]Km+[S]=10KmKm+10Km=1011=0.90

Conclusion

Conclusion:

The fractions of Vmax at different substrate concentration is 0.33, 0.66 and 0.90.

(c)

Summary Introduction

To determine: The different curves corresponds to which enzyme.

Introduction:

Enzyme is a biological macromolecule that acts as a catalyst and enhance rate of chemical reactions. Various biological processes are dependent on enzyme. All enzymes have an active site on to which amino acids of proteins get binds and form an enzyme-substrate complex.

(c)

Expert Solution
Check Mark

Explanation of Solution

Explanation:

The upper curve indicates enzyme B as [X] is greater than Km of enzyme while lower curve indicates enzyme A as the [X] is smaller than Km of enzyme.

It can be concluded that if the rate of initial concentration of substrate is greater than Km then rate of chemical reaction is less sensitive to conversion of substrate at initial stage of reaction. So rate of reaction is linear for longer period of time.

Conclusion

Conclusion:

In the given graph, upper curve corresponds to enzyme B whereas lower curve corresponds to enzyme A.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!
Students have asked these similar questions
Biochemistry What is the process of "transamination" in either the muscles or the liver, that involves keto acid or glutamic acid? Please explain how the steps work. Thank you!
Biochemistry Please help. Thank you What is the importance of glutamic acid in the metabolism of nitrogen from amino acids? (we know therole; it’s used to remove the nitrogen from amino acids so that the remaining carbon skeleton can bebroken down by the “usual” pathways, but what is the important, unique role that only glutamicacid/glutamate can do?)
Biochemistry Please help. Thank you When carbamyl phosphate is joined to L-ornathine, where does the energy for the reaction come from?
Knowledge Booster
Background pattern image
Biochemistry
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
Text book image
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Text book image
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Text book image
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Text book image
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Text book image
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License