Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN: 9781305389892
Author: Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher: Cengage Learning
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Chapter 2, Problem 14TYK
Summary Introduction
To explain:
The substance that can be added to the reaction mixture to maintain a high activity of the enzyme, with the reason for the same.
Introduction:
The acidic or basic character is expressed in terms of pH (potential of hydrogen). It is a negative logarithm of the concentration of
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enzymes are naturally occurring catalysts responsible for various biochemical reactions. Give a modern and recent application of an enzyme used in a biochemical reaction
a - the commercial or trade name of the catalyst and enzyme.
b - the properties of the catalyst and enzyme (e.g., shape, size, colour, price).
c - the advantages and the disadvantages of the chosen catalyst and enzyme
d - catalytic reaction (e.g., the reactant, product, reaction equation, phase, selectivity, promoter, catalyst support, operating temperature & pressure).
Imagine you are working in a lab, and you are performing two chemical reactions. You
notice that Reaction A occurs much faster than Reaction B, and that both reactions
release the same amount of heat. Which of the following conclusions can be made
from your observation?
Reaction A has the same activation energy as Reaction B, and the AG of
Reaction A is more negative (i.e., a larger negative number) than the AG for
Reaction B.
Reaction A has a lower activation energy than Reaction B, and the AG of
Reaction A is the same as the AG of Reaction B.
Reaction A has a higher activation energy than Reaction B, and the AG of
Reaction A is the same as the AG of Reaction B.
Reaction A has the same activation energy as Reaction B, and the AG of
Reaction A is less negative (i.e., a smaller negative number) than the AG for
Reaction B.
Enzyme kinetics uses math to quantify all of the following, except:
a. An enzyme's substrate affinity
b. None; all the other choices are correct
OC.
An enzyme's catalytic power
Od. An enzyme's stability
Chapter 2 Solutions
Biology: The Dynamic Science (MindTap Course List)
Ch. 2.1 - Distinguish between an element and an atom, and...Ch. 2.2 - Prob. 1SBCh. 2.2 - Prob. 2SBCh. 2.2 - Prob. 3SBCh. 2.3 - Prob. 1SBCh. 2.3 - Prob. 2SBCh. 2.3 - Prob. 3SBCh. 2.3 - Prob. 4SBCh. 2.4 - Prob. 1SBCh. 2.4 - Prob. 2SB
Ch. 2.5 - Prob. 1SBCh. 2.5 - Why are buffers important for living organisms?Ch. 2 - Which of the following statements about the mass...Ch. 2 - Oxygen (O) is a(n) _______; the oxygen we breathe...Ch. 2 - The chemical activity of an atom: a. depends on...Ch. 2 - When electrons are shared equally between atoms,...Ch. 2 - Which of the following is not a property of water?...Ch. 2 - The water lattice: a. is formed from hydrophobic...Ch. 2 - A hydrogen bond is: a. a strong attraction between...Ch. 2 - Apply Evolutionary Thinking What properties of...Ch. 2 - If pond water has a pH of 5, the hydroxide...Ch. 2 - Prob. 10TYKCh. 2 - Prob. 11TYKCh. 2 - Prob. 12TYKCh. 2 - Discuss Concepts You place a metal pan full of...Ch. 2 - Prob. 14TYKCh. 2 - Prob. 15TYKCh. 2 - The pH of human stomach acid ranges from 1.0 to...Ch. 2 - Prob. 2ITDCh. 2 - Prob. 3ITD
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- Chemistry (True / False) A researcher speculates that an enzyme has the following energy profile and that it is a reasonable profile given what we know about enzyme behavior. Enzyme bound to Substrate: -7.00 kcal/mol Enzyme bound to Product: -10.00 kcal/mol Enzyme in transition state: -5.00 kcal/mol Why would the answer be false?arrow_forwardHow does the average reaction rate differ from an instantaneous reaction rate? © A. The average reaction rate is how quickly the reaction proceeds over time. An instantaneous reaction rate is how quickly the reaction proceeds at a specific time. B. The average reaction rate is how quickly the reaction proceeds at a specific time. An instantaneous reaction rate is how quickly the reaction proceeds over time. C. The average reaction rate is how quickly the reaction proceeds over time considering the reactants. An instantaneous reaction rate is how quickly the reaction proceeds at a specific time considering the products. D. The average reaction rate is how quickly the reaction proceeds over time. An instantaneous reaction rate is how quickly the reaction proceeds compared to another reaction.arrow_forwardPredict the missing reactant of this biochemical reaction: anatate.. CH3 C CH₂¯ X Pi + H₂O That is, in the drawing area below, draw the chemical structure of the reactant molecule X. Note for advanced students: you can assume any necessary small-molecule reactants, like water, are available. Click and drag to start drawing a structure. X :0 Śarrow_forward
- Find kcat for a reaction in which Vmax is 4 × 10-4 mol•min-1 and the reaction mixture contains one microgram of enzyme (the molecular weight of the enzyme is 200,000 D). Show your work/reasoning.arrow_forwardWhich of the following statements are true for BOTH the "transition state" and an "intermediate" of reaction? (This is a multi-select question, select all that apply.). Both are only observed in enzyme-catalyzed reactions. Both can be converted to product(s) or might decompose back to the reactant(s). Neither are part of the "net equation" for the reaction. Both contain covalent bonds are in the process of breaking and/or forming. Both are part of every chemical reaction. (i.e. the mechanisms of all chemical reactions, whether enzyme catalyzed or not, will have involve both a transition state and an intermediate).arrow_forwardWhich statements are true and which are false? Modify each false statement so that it reads correctly. a. In a closed system, neither energy nor matter is exchanged with the surroundings. b. State functions are independent of the pathway. c. A process is isothermic if ΔH = 0. d. The sign and magnitude of ΔG give important information about the direction and rate of a reaction. e. At equilibrium, ΔG = ΔG°. f. For two reactions to be coupled, they must have a common intermediate.arrow_forward
- Drag and drop the statements to the correct box: Enzymes DO: Decrease required activation energy Enzymes DON'T: Remain unchanged during the reaction Increase the reaction rate Energy Change the products made Activation energy (X+Y) reactants Change the reactants used Activation Energy A Activation energy (Y→X) products ΔΗ Reaction path Reaction without catalyst Reaction with catalyst Name two things we learned that can denature an enzyme:arrow_forwardWhat is the difference between biochemical, pharmaceutical, and diagnostic chemical reactions? What is a specific example that exists for each and why might they be important to healthcare professionals? List a balanced chemical equation for each and explain how it is used in your example above.arrow_forwardAn enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation. SHOW MORE The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d The Vmax for X will be affected if Y is present in the reaction mixture. pH dependence of Vmax reflects the ionization state of catalytic site residues. e Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X= 0.01 M and the Km f for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of products to reactants (Ken). A mutation in the active site of an enzyme resulting in a large increase in…arrow_forward
- What statements concerning free energy change are true or false? a. Free energy change is a measure of the rate of a reaction. b. Free energy change is a measure of the maximum amount of work available from a reaction. c. Free energy change is a constant for a reaction under any conditions. d. Free energy is related to the equilibrium constant for a specific reaction. e. Free energy change is equal to zero at equilibriumarrow_forwardA. Will decreasing the amount of energy needed to make an exergonic reaction occur cause the reaction to be more exergonic? Why or why not? B. Will such an energetic alteration change the rate of the reaction? Why or why notarrow_forwardBriefly discuss three (3) reasons why enzyme reactions are better than its chemical reactions counterparts.arrow_forward
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