(b) Determine how the reaction rate varies with substrate concentration. Rate increases substrate is added when enzyme is saturated with substrate Incorrect Rate decreases additional substrate is added when substrate concentration is low Answer Bank Rate is unchanged additional substrate is added when substrate concentration is very high

(b) Determine how the reaction rate varies with substrate concentration. Rate increases substrate is added when enzyme is saturated with substrate Incorrect Rate decreases additional substrate is added when substrate concentration is low Answer Bank Rate is unchanged additional substrate is added when substrate concentration is very high

General, Organic, and Biological Chemistry

7th Edition

ISBN:9781285853918

Author:H. Stephen Stoker

Publisher:H. Stephen Stoker

Chapter21: Enzymes And Vitamins

Section: Chapter Questions

Problem 21.49EP

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Similar questions

Based on the graphical information in Problem 21-41 about enzymes A and B indicate whether the enzyme activity of enzyme B increases or decreases when the following changes in reaction conditions are made. a. pH decreases from 7.6 to 7.2 b. pH increases from 7.2 to 7.4 c. temperature decreases from 37.8C to 37.6C d. temperature increases from 38.2C to 38.4C
The human body has an average pH of about 7 and a temperature of about 37C. Use graphs to illustrate enzyme activity in the human body as a function of the following: a. Substrate concentration b. Enzyme concentration c. pH include pH optimum value d. Temperature include temperature optimum value
When handling or storing solutions of enzymes, the pH is usually kept near 7.0. Explain why.
The site on an enzyme molecule that does the catalytic work is called the: a. binding site. b. allosteric site. c. lock. d. active site.
The process by which an enzyme acts on the substrate can be described by the: a. lock-and-key model. b. enzyme-and-substrate model. c. enzyme folding model. d. catalytic model.
Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
All of the following are reasons for considering the enzymes as druggable targets except: O enzymes have the allosteric sites where modulators can bind O it is easy to purify in significant amount and characterize the enzymes O enzyme kinetics concepts are well established for identifying inhibitors and activators O hits and leads can be identified from known substrates and transition-states
Oxaloacetate is an inhibitor of succinate dehydrogenase because it is structurally very similar to succinate as shown below. Also, its binding to the enzyme does not involve any covalent bond formation. What type of inhibitor is oxaloacetate? COO | CH₂ 1 CH₂ 1 COO Succinate COO | CH₂ C=O COO Oxaloacetate O a noncompetitive inhibitor both a noncompetitive and an irreversible inhibitor O an irreversible inhibitor O a competitive inhibitor
Why do we say the two enzyme-catalyzed reactions taking place in your test tube are "coupled"? O peroxidase and glucose oxidase utilize hydrogen peroxide as a substrate O peroxidase utilizes the lactone produced by glucose oxidase as a substrate O because there is a dye in solution O peroxidase and glucose oxidase utilize glucose as a substrate Operoxidase utilizes the hydrogen peroxide produced by glucose oxidase as a substrate Evaluate
How does the metal ion in carboxypeptidase A increase the enzyme’s catalytic activit
What do we mean when we say an enzyme is saturated with substrate? When an enzyme is saturated with substrate, how does adding more (a) substrate and (b) enzyme affect the rate of the reaction?
Substrate Enzyme-substrate complex 1. Is this an example of a lock & key or induced fit model of an enzyme? > Enzyme