Becker's World of the Cell (9th Edition)
Becker's World of the Cell (9th Edition)
9th Edition
ISBN: 9780321934925
Author: Jeff Hardin, Gregory Paul Bertoni
Publisher: PEARSON
bartleby

Concept explainers

bartleby

Videos

Textbook Question
Book Icon
Chapter 6, Problem 6.5PS

Michaelis–Menten Kinetics. Figure 6-16 represents a Michaelis–Menten plot for a typical enzyme, with initial reaction velocity plotted as a function of substrate concentration. Three regions of the curve are identified by the letters A, B, and C. For each of the statements that follow, indicate with a single letter which one of the three regions of the curve fits the statement best. A given letter can be used more than once.

Chapter 6, Problem 6.5PS, MichaelisMenten Kinetics. Figure 6-16 represents a MichaelisMenten plot for a typical enzyme, with

Figure 6-16 Analysis of the Michaelis–Menten Plot. See Problem 6-5.

  1. (a) The active site of an enzyme molecule is occupied by substrate most of the time.
  2. (b) The active site of an enzyme molecule is free most of the time.
  3. (c) This is the range of substrate concentration in which most enzymes usually function in normal cells.
  4. (d) This includes the point (Km, Vmax/2).
  5. (e) Reaction velocity is limited mainly by the number of enzyme molecules present.
  6. (f) Reaction velocity is limited mainly by the number of substrate molecules present.
Blurred answer
Students have asked these similar questions
. Recall your study of equilibria and kinetics from general chemistry. You used equations with upper case Kand lower case k during the study of equilibria and kinetics respectively. What do the upper and lower case letters refer to?
Enzyme Action: Testing Catalase Activity 8) Explain why the [VO] of the reactions at pH 3 and temperature of 100'C were (or should have been) tower than the other treatments conducted. In your response consider the following: a) The effect of these conditions on the structure of the enzyme. b) Why this structural effect resulted in a decreased [VO].
6-25 substrate-band enzyme concentrations. The the turnover number is equal to umax- b) V=Umax •57(Km+S) anstont For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM C) d) e) [S] = 0.5KM [S] = = 0.1KM [S] = 2KM [S] = 10KM w reactores -maximumrate of reaction boteles conc. Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?
Knowledge Booster
Background pattern image
Biology
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
Text book image
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Text book image
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Text book image
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
Text book image
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company
Text book image
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
Text book image
Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education
Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License