. The following data, presented by G. Bowes and W. L. Ogre in J. Biol.Chem. (1972) 247:2171–2176, describe the relative rates of incorpo-ration of CO, by rubisco under N, and under pure O,. Decidewhether O, is a competitive or uncompetitive inhibitor.[CO,] (mM)Under N2Under O,0.2016.7100.1012.55.60.0678.34.20.0507.13.2

Enzyme inhibition refers to a decrease in enzyme related processes, enzyme production, or enzyme…

Answered: . The following data, presented by G.…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

How was thermal stability measured in this paper and describe how GRL-1720 and 5h affect the thermal stability of Mpro and which drug has the larger effect? https://www.nature.com/articles/s41467-021-20900-6
A bacterial culture is grown using either octadecane (C18H38) or pentachlorophenol (C6HCl5O) as the sole source of carbon and energy. The cell yield value is determined by dry weight analysis to be 1.49 for octadecane and 0.05 for pentachlorophenol. Using either octadecane or pentachlorophenol, please describe the steps taken (and the final result) showing what percentage of the substrate carbon will be found as cell mass and as CO2? Please show all calculations.
Using equilibrium argument, why does Km apparently increase, decrease or stay the same in uncompetitive inhibition?
Please answer A & B attached with image.
6. The Vmax and KM values for an unusual hexokinase found in Try- pansoma cruzi (the causative agent of Chagas disease) are shown in the presence and absence of a bisphonate inhibitor (structure shown). Without inhibitor With inhibitor Км (mM) 90 125 Vn max (umol min-1. mL-1) 0.30 0.12 ОН O=P-O- A bisphonate compound a. What type of inhibitor is bisphonate? b. The parasite hexokinase, unlike the mammalian enzyme, is not inhibited by glucose-6-phos- phate but is inhibited by pyrophosphate (PP;). Is this observation con- sistent with your answer to part a? c. Might bisphonate be a good candidate for a drug to treat the disease?
The problem set question is below. In the image
Vmax [S] Km + [S] Vo = Eadie-Hofstee plot Lineweaver-Burk (L-B) plot v=Vm-Km [S] Km 1 Vm Vm [S] 1 The equations above apply for Michaelis-Menten enzyme kinetics but are presented in three different formats. For uncompetitive inhibition The Michaelis-Menten equation becomes Vo-Vmax(S)/(Km+a'[S)) Put the Minchaelis-Menten equation for uncompetitive inhibition in the Lineweaver-Burk format. The slope of this plot will be
Calculate the Km of the maltase reaction with inhibitor X (If inhibitor X changes maltase activity to a Vo of 0.10 mM per minute when [S] = 0.125 mM, and a Vo of 0.25 mM per minute when [S] = 0.50 mM). 0.10 mM 0.20 mM 0.50 mM 1.0 mM 2.0 mM
Noncompetitive inhibition can often be explained by which of the following models? the induced fit model the lock and key model both (a) and (b) neither (a) nor (b)
An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.
you are trying to come up with a drug to inhibit the activity of an enzyme thuogth to have a role in a liver disease. in the lab the enzyme was shown to have a Km of 1x10-6 M and Vmax of 0.1 micromoles/min.mg measruing at room temperature. you developed a mixed non-competitve inhibitor with a ki=0.4x10-6M and a Ki` pf 0/2 x 10-5 What will be the apparent Km in the presence of 1.0x10-6 M?
(a) You are given the following experimental measurements for the effects of an inhibitor on the initial velocity of an enzymatic reaction. Plot the data and determine what type of inhibition is being observed. Label all axes. [S] (MM) Vo (mM • Vo with I present (mM ⚫s-¹) 1 2.8 3 6.0 1.0 2.5 4 7.0 3.1 8 9.9 12 11.5 4.8 5.7 (b) Briefly explain how varying [S] can be used to determine whether an inhibitor is uncompetitive or competitive. Be sure to include in your explanation why this method would work.

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS