You are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is theV, dependant on if the concentration of the substrate is substantially higher than the concentrationof the enzyme?[S][E][ES]O [P]O not enough information provided

The general reaction equation of the ,Michaelis - Menten equation is E+S ----k1--->[ES]…

Answered: You are working on an enzyme that obeys…

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

An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each substrate concentration. [S] = 1.75 mM MM-s-1 [S] = 7.50 mM [S] = 11.0 mM DO mM-s mM-s
At what substrate concentration would an enzyme with a kcat of 33.0 s-1 and a Km of 0.0046 M operate at one-tenth of its maximum rate? Assume the enzyme obeys Michaeli s-Menten kinetics.
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…
You are working on an enzyme that obeys standard Michaelis-Menten kinetics. You have determined the Vmax to be 0.1 mol/sec and the Km to be 2.5 mM. What would the rate of the reaction be when the substrate concentration is 20 mM? 0.09 MS-1 O 0.133 Ms-1 O 0.18 Ms ¹ 9 Ms-1 O 0.018 Ms-1 0.2 MS-1
(i) Which graph indicates an enzymatic reaction without inhibitor?(ii) Which type of inhibitor is it? Briefly explain.(iii) Which graph indicates the highest concentration of inhibitor?(iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers.
How is it possible to determine the structure of an enzyme substrate complex by x ray crystallography when the reaction is over so quickly and the x ray analysis takes at least several minutes?
Create a ONE page, formal summary, including APA Formatted in-text citations, of the enzyme amalyze and how it is used in the meat processing industry (Address all guiding questions below in your summary). Note, references can be the second page of the assignment. Include the questions in ur answer Which enzyme is used in the industry (if more than one enzyme is included, you can choose one of the enzymes) Describe the molecular structure of the enzyme (how many amino acids; discuss different levels of protein structure-secondary, tertiary, quaternary, key structural components/amino acids in active site) Describe how the enzyme works in the industry and why it is a key component for this industry. What specific reaction(s) are being catalyzed? What types of bonds are being broken?
How temperature, pH and salt affects the enzyme activity in terms of protein structure (primary, secondary, tertiary, quaternary) and other factors? Please explain briefly.
How can you find Kcat if you are only given Vmax, Km and [E] ? I tried using Kcat=Vmax/[E] but that didn't work. How do you know if [E] is the same as [E]total, and if it isn't how do you find it from this information: The Vmax for a particular enzyme is 10 nmols/L/s. The Km for its substrate is 5 microM. If the enzyme concentration is 10 nM, what is the kcat? a.80 nmoles/L/s b.8000 nmoles/L/s c.2 nmoles/L/s d.50 nmoles/L/s
Using the appropriate graph and table above, explain what the R48C mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.
The following data was obtained during kinetic analysis of an enzyme with and without an inhibitor. Substrate concentration (mM) Reaction rate without inhibitor (µM/s) Reaction rate with inhibitor (µM/s) 10 28 12 20 50 23 40 83 42 60 107 58 100 139 83 200 179 125 300 197 150 400 209 167 560 227 197 How do you calculate the KM for the enzyme in the absence of an inhibitor. And how do you calculate kcat with the given enzymatic concentration of 5 µM.
82.16

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

You are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is the V, dependant on if the concentration of the substrate is substantially higher than the concentration of the enzyme? [S] O [ES] O [P] not enough information provided