Seeley's Anatomy & Physiology
11th Edition
ISBN: 9781259254963
Author: Jennifer Regan (author), Andrew Russo (author), Rod Seeley (author) Cinnamon Vanputte (author)
Publisher: McGraw Hill Higher Education
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Chapter 2, Problem 23RAC
Summary Introduction
Introduction:
Enzymes are proteins that play various roles in the body. An enzyme can increase the
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Which of the following accurately characterizes enzyme active sites? (Pick two.)
Active sites form the greatest number of favorable electrostatic interactions with a reaction's
substrates.
Active sites form the greatest number of favorable electrostatic interactions with a reaction's
transition state.
Competitive inhibitors that resemble an enzyme's substrate bind more tightly to the active site than
those that resemble products or transition states.
Competitive inhibitors that resemble an enzyme's transition state bind more tightly to the active site
than those that resemble products or substrates.
Which of the following is NOT true about enzymes?
Enzyme inhibitors interact reversibly or irreversibly with an enzyme to alter its Km and /or Vmax values.
Enzymes typically act under milder conditions of temperature and pH than non-enzyme chemical catalysts.
Zymogens are the inactive precursors of enzyme.
Nucleophilic groups can catalyze reactions through the transient formation of covalent bonds with the substrate.
Transition state stabilization can significantly increase the activation energy for a reaction.
An inhibitor was added to an enzyme and the expected rate of the reaction was not detected and the substrate was not utilized at all. This inhibitor is (choose one answer only):
Is un-competitive, meaning the inhibitor binds to a site near the active site.
Is competitive, meaning the inhibitor binds directly to the same active site as the subtrate.
Is non-competitive, meaning the inhibitor binds to site other than the active site as the subtrate.
Is irreversible, meaning the inhibitor binds covalently to the enzyme keeping the enzyme inactive permanently.
Chapter 2 Solutions
Seeley's Anatomy & Physiology
Ch. 2.1 - Define matter. How are the mass and the weight of...Ch. 2.1 - Differentiate between element and atom. What four...Ch. 2.1 - Prob. 3AYPCh. 2.1 - Which subatomic particle determines the atomic...Ch. 2.1 - What is an isotope? How are isotopes denoted?Ch. 2.1 - What is avogardro’s number? How is it related to a...Ch. 2.1 - Describe how an ionic bond is formed. What are...Ch. 2.1 - What occurs in the formation of a covalent bond?...Ch. 2.1 - Distinguish between a molecule and a compund. Give...Ch. 2.1 - What are intermolecular forces, and how do they...
Ch. 2.1 - What is meant by the statement “table sugar is...Ch. 2.1 - Describe what occurs during the dissociation of...Ch. 2.1 - Explain the difference between electrolytes and...Ch. 2.2 - Using the terms reactant and product, describe...Ch. 2.2 - Contrast synthesis and decomposition reactions,...Ch. 2.2 - Describe the role of water in dehydration and...Ch. 2.2 - What is a reversible reaction? How does this type...Ch. 2.2 - What are oxidation-reduction reactions?Ch. 2.2 - Define energy. How are potential and kinetic...Ch. 2.2 - Summarize the characteristics of mechanical,...Ch. 2.2 - Use ATP and ADP to Illustrate the release or input...Ch. 2.2 - Define activation energy, catalyst, and enzymes;...Ch. 2.2 - What effect does increasing temperature or...Ch. 2.3 - What is the difference between inorganic and...Ch. 2.3 - What two properites of water are the result of...Ch. 2.3 - List and briefly describe the four functions that...Ch. 2.3 - Prob. 27AYPCh. 2.3 - Prob. 28AYPCh. 2.3 - Prob. 29AYPCh. 2.3 - Prob. 30AYPCh. 2.3 - Prob. 31AYPCh. 2.3 - Prob. 32AYPCh. 2.3 - Prob. 33AYPCh. 2.3 - Prob. 34AYPCh. 2.3 - What are the functions of oxygen and carbon...Ch. 2.4 - Prob. 36AYPCh. 2.4 - Prob. 37AYPCh. 2.4 - Prob. 38AYPCh. 2.4 - Prob. 39AYPCh. 2.4 - Which carbohydrates are used for energy? What is...Ch. 2.4 - Prob. 41AYPCh. 2.4 - Prob. 42AYPCh. 2.4 - Prob. 43AYPCh. 2.4 - Prob. 44AYPCh. 2.4 - Prob. 45AYPCh. 2.4 - Prob. 46AYPCh. 2.4 - What are the building blocks of proteins? What...Ch. 2.4 - Prob. 48AYPCh. 2.4 - Prob. 49AYPCh. 2.4 - Compare the lock-and-key and the induced fit...Ch. 2.4 - Prob. 51AYPCh. 2.4 - What are the basic building blocks of nucleic...Ch. 2.4 - DNA is like a twisted ladder. What forms the sides...Ch. 2.4 - Prob. 54AYPCh. 2.4 - Prob. 55AYPCh. 2.4 - Prob. 56AYPCh. 2.4 - Prob. 57AYPCh. 2 - Prob. 1RACCh. 2 - Prob. 2RACCh. 2 - Prob. 3RACCh. 2 - Prob. 4RACCh. 2 - Table salt (NaCl) is an atom organic. a molecule....Ch. 2 - Prob. 6RACCh. 2 - Prob. 7RACCh. 2 - Prob. 8RACCh. 2 - Prob. 9RACCh. 2 - Prob. 10RACCh. 2 - Prob. 11RACCh. 2 - Which of these statements concerning enzymes is...Ch. 2 - Prob. 13RACCh. 2 - Prob. 14RACCh. 2 - Prob. 15RACCh. 2 - Prob. 16RACCh. 2 - A buffer slows down chemical reactions. speeds up...Ch. 2 - Prob. 18RACCh. 2 - Prob. 19RACCh. 2 - Prob. 20RACCh. 2 - Prob. 21RACCh. 2 - Prob. 22RACCh. 2 - Prob. 23RACCh. 2 - DNA molecules conatin genes. contain a single...Ch. 2 - Prob. 25RACCh. 2 - Prob. 1CTCh. 2 - Prob. 2CTCh. 2 - A mixture of chemicals is warmed slightly. As a...Ch. 2 - Two solutions, when mixed together at room...Ch. 2 - Prob. 5CTCh. 2 - Prob. 6CTCh. 2 - Carbon dioxide that accumulates in the blood can...Ch. 2 - An enzyme (E) catalyzes the following reaction:...Ch. 2 - Using the materials commonly found in a kitchen,...
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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
- Which of the following are effects of catalyst that cause an increase in the rate of reaction? (This is a multi-select question. Select all that apply). a decrease in DG‡. an increase in DG. an increase in temperature. an increase in the energy of the molecules/ions of reactant. an increase in the number of molecules/ions of reactant with enough energy to overcome the activation energy barrier.arrow_forwardHomeostasis is important for all of the functions of the human body. Why is maintaining homeostasis important for enzymes? Group of answer choices: To maintain their normal structure and function To prevent substrate from binding to the enzyme To allow the substrate to bind forever To cause the enzyme to fold differently for each reactionarrow_forwardTwo substrates (A and B) are used to produce a certain biological product in an enzyme- catalyzed reaction. It is found that both substrates must bind to the enzyme, first Substrate A, then Substrate B before the product is produced. What kind of kinetic mechanism is described? Linear Reaction Ordered Sequential Reaction Random Sequential Reaction Ping Pong Reactionarrow_forward
- Another of the six enzyme classes is which of the following? enzymes catalyze. These classes include the transferases, isomerases, and ligases. All enzymes can be categorized in one of six major classes based on the reactions the proteases kinases hydrolases phosphatases endonucleases An important factor that influences the rate of a biochemical reaction is the temperature. Raising the temperature of a biochemical reaction has which effect upon the kinetics of the reaction? a) b) c) d) e) increases the free energy of the reactants increases the free energy of the transition state decreases the free energy of the reactants decreases the free energy of the transition state decreases the free energy of the productsarrow_forwardwhich of the following describes an enzyme ALLOSTERIC site?arrow_forwardA transition-state analog— resembles the active site of general acid-base enzymes. is less stable when binding to an enzyme than the normal substrate. stabilizes the transition state for the normal enzyme-substrate complex. reacts more rapidly with an enzyme than the normal transition state intermediate. resembles the transition-state structure of the normal substrate in the enzyme-substrate complex.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_forwardAmylase is an enzyme found in saliva that breaks down starch. The enzyme is currently functioning at its optimal pH of 7 and optimal temperature of 32oC. Which of the following could result in an increase in the reaction rate? Providing an environment with a pH of 9. Decreasing enzyme concentration. Placing the reactants in an environment at 10oC. Increasing substrate concentration.arrow_forwardWhich of the following is correct regarding enzymes? Enzymes can speed up the rate of reaction by shifting the equilibrium of the reaction forward. Enzymes can make a nonspontaneous reaction spontaneous. Most enzymes are made up of DNA and RNA and are named based on the reaction that they catalyze. Enzymes can increase the rate of a reaction, but do not shift the equilibrium of a reaction.arrow_forward
- Which of the following statements describes a dimeric allosteric enzyme following the concerted model? The RR form of the enzyme is the most active. The equilibrium between the T state and R state favors the T state. The enzyme can exist as an RT dimer. The enzyme can exist as an RR dimer.arrow_forwardIndicate whether each of the following statements about an enzyme active site is true or false. It is the location where substrate molecules are produced. It always has a fixed, rigid geometry. It always has a geometrical shape exactly complementary to that of substrate. It always accommodates several structurally related substrates. It is the location where substrate molecules are converted to product molecules. It always has a shape that has a degree of flexibility to it. It always accommodates only one specific substrate.arrow_forwardinfarrow_forward
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