Life: The Science of Biology
11th Edition
ISBN: 9781319010164
Author: David E. Sadava, David M. Hillis, H. Craig Heller, Sally D. Hacker
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 8.4, Problem 3R
Summary Introduction
To review:
The shape of the curve, when
Introduction:
Enzymes catalyze biological reactions at a faster velocity. They achieve this by combining substrate molecules at their active site and stabilizing complex, and in this process they lower the activation energy. Each enzyme is unique to its substrate molecule by the virtue of its active site. The enzymes on binding with substrate convert them into products and made available to bind with other molecules to carry out the same reaction.
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
Indicate i) the class of enzymes to which it belongs to, ii) name the kind of bond that is modified due to its activity, iii) indicate the substrate that is recognised by the enzyme using the amino acid three letter code and iv) whether the enzyme displays high or low substrate specificity. Must be less than 50 words total.
An enzymatic reaction was carried out in a batch-operated reactor until exhaustion of the substrate. The formation of the product was monitored over time, obtaining the results shown in Table 1. Answer:
a) Knowing that the initial substrate concentration was 0.2 M and that the stoichiometry reaction is: 1S –> 2P, estimate the substrate concentration over time from the data from [P] data in Table 1;
b) Determine the parameters of the Michaelis-Menten equation, Vmax and Km, by fitting direct from the hyperbola function;
c) Determine the parameters Vmáx and Km, by the linearized equation;
Most enzymes have optimum operating conditions to function at maximum rate or velocity. Some of these conditions are the pH temperature the enzyme concentration and the substrate concentration. The optimum pH and temperature values for most enzymes are:
a) pH of 1.0 and + 100 oC
b) pH of 11.0 and - 7 oC
c) pH of 7.0 and + 37 oC
d) pH of 14.0 and + 370 oC
e) None of the above
Chapter 8 Solutions
Life: The Science of Biology
Knowledge Booster
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
- Based on the kinetic constants below, which enzyme will most efficiently catalyze conversion of the substrate into product? A) Vmax = 10 uM s-1, KM = 10 µM B) Vmax = 10 uM s-1, KM = 0.01 µM C) Vmax = 1000 uM s-1, KM = 500 µM D) Vmax = 1 uM s-1, KM = 1 µM E) Vmax = 200 uM s-1, KM = 10 µMarrow_forwardExplain why the maximum initial reaction rate cannot be reached at low substrate concentrations.arrow_forwardPlease handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.arrow_forward
- Enzyme specificity us given by :- а) Km b) Vmax c) both d) nonearrow_forwardDescribe the formation of bioprocess product. Please include the following: (a) Product of choice and Raw materials and microorganism (b) Step by step processes using flow chart (including process condition; ie, temperature, 02) (C) Detail drawing of unit operations involved (include upstream and downstream unit operation)arrow_forwardVmax for an enzyme-catalyzed reaction: A) generally increases when pH increases. B) is limited only by the amount of substrate supplied. C) is twice the rate observed when the concentration of substrate is equal to the Km. D) is unchanged in the presence of a uncompetitive inhibitor. E) increases in the presence of a competitive inhibitor.arrow_forward
- Part a) Which graph has the largest kcat? Please explain. Part b) Which graph has the tightest substrate binding? Please explain. Part c) Which graph has the largest specificity or efficiency constant? Please explain.arrow_forwardBriefly describe the series of events must take place between the binding of substrate to enzyme, and the re-appearance of free enzyme and product.arrow_forwardVmax for an enzyme-catalyzed reaction: A)is twice the rate observed when the concentration of substrate is equal to Km. B)is unchanged in the presence of a noncompetitive inhibitor. C)generally increases when pH increases. D)increases in the presence of a competitive inhibitor. E)is limited only by the amount of substrate supplied.arrow_forward
- 14) Which of the following statements is true under the conditions provided: the enzyme concentration is 0.5 nM, substrate concentration is 10 µM, and the KM = 20 µM? a) The enzymatic reaction occurs at maximal velocity. b) The enzymatic reaction occurs between half-maximal and maximal velocity. c) The enzymatic reaction occurs at around half-maximal velocity. d) The enzymatic reaction occurs at between zero and half-maximal velocity. e) Not enough information given to know about the enzymatic reaction rate.arrow_forward1. When the velocity of enzyme activity is plotted against substrate concentration, which of the following is obtained? a) Straight line with negative slope b) Straight line with positive slope c) Parabola d) Hyperbolic curvearrow_forwardGive typing answer with explanation and conclusion Which of the following is true under the following conditions: The enzyme concentration is 8 nM, the substrate concentration is 8 mM, and the KM is 8 μM.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSON
Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
Anatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
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
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
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