Microbiology: Principles and Explorations
9th Edition
ISBN: 9781118743164
Author: Jacquelyn G. Black, Laura J. Black
Publisher: WILEY
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Chapter 5, Problem 8SQ
Summary Introduction
To examine: Whether the statement, “the enzyme cofactors are usually inorganic ions that enhance enzymatic activity by improving the “fit” between an enzyme and its substrate”, is true or false.
Introduction: The enzymes are the protein molecules that are synthesized by the cells of the living organisms. They act as biological catalysts to speed up the biochemical processes in the cell, but it is not used up in the process and can be used over again and again.
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Enzymes are proteins that increase the rate of chemical reactions by lowering the energy activation required to facilitate the process. Explain the generalized and sequential enzyme mechanism of action (hint: from substrates to products).
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If the ATP-binding site of an enzyme is buried in the interior of the enzyme, in a hydrophobic environment, is the ionic interaction between enzyme and substrate stronger or weaker than that same interaction would be on the surface of the enzyme, exposed to water? Why?
Chapter 5 Solutions
Microbiology: Principles and Explorations
Ch. 5 - How are photosynthesis and respiration related to...Ch. 5 - What is the main difference between...Ch. 5 - Distinguish between coenzyme and cofactor. How are...Ch. 5 - Prob. 2.2SCCh. 5 - Prob. 3.1SCCh. 5 - If four actual molecules of ATP are produced for...Ch. 5 - Prob. 3.3SCCh. 5 - Prob. 3.4SCCh. 5 - Prob. 4.1SCCh. 5 - What is returned to chlorophyll in cyclic...
Ch. 5 - What were probably the first kind of...Ch. 5 - What type of metabolism is characteristic of...Ch. 5 - Prob. 1CCSCh. 5 - Suppose that you had a culture known to contain...Ch. 5 - In what sequence might the different kinds of...Ch. 5 - Prob. 3CTQCh. 5 - Which of the following is not true about...Ch. 5 - Prob. 2SQCh. 5 - Prob. 3SQCh. 5 - Prob. 4SQCh. 5 - Prob. 5SQCh. 5 - Prob. 6SQCh. 5 - Prob. 7SQCh. 5 - Prob. 8SQCh. 5 - All of the following statements about competitive...Ch. 5 - Prob. 10SQCh. 5 - What is feedback inhibition? (a) When the end...Ch. 5 - Which of the following is true regarding the...Ch. 5 - Prob. 13SQCh. 5 - Prob. 14SQCh. 5 - During aerobic cell respiration most of the energy...Ch. 5 - The typical end products of complete aerobic cell...Ch. 5 - Prob. 17SQCh. 5 - The end products of photosynthesis in...Ch. 5 - Which of the following final electron acceptors is...Ch. 5 - Prob. 20SQCh. 5 - Prob. 21SQ
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- which of the following is a primary function of the active site of an enzyme?arrow_forwardOne way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. Enzyme Substrate Turnover number (per second) Ribonuclease RNA 100 Fumarase fumarate 800 Lactate dehydrogenase lactate 1000 Urease urea 10,000 How many molecules of urea can one molecule of urease act on in 12.0 min ?arrow_forwardWhen lead acts as a poison, it can do so either by replacing another ion (such as zinc) in the active site of an enzyme or by reacting with cysteine side chains to form covalent bonds. Which of these is irreversible and why? Match the items in the left column to the appropriate blanks in the sentences on the right. Reset Help a covalent bond When occurs between the active site (containing cystein) and the inhibitor (lead), replacement of an ion the substrate is excluded or the catalytic reaction is blocked. an ionic bond When occurs and the inhibitor (lead) replaces another ion. reaction with side chains The is an example of a permanent, irreversible change. ion exchange The is an example of a change that can be reversed.arrow_forward
- Define the word "enzyme inhibition."arrow_forwardDescribe the reactants and products of the following enzyme catalyzed reaction. Names of molecules are sufficient.arrow_forwardAn inactive form of an enzyme becomes active after being phosphorylated. When glucose is converted to glucose-6-phosphate by hexokinase, the accumulation of glucose-6-phosphate inhibits the reaction. A foreign substance is added to the reaction above. This substance binds to hexokinase and prevents its ability to catalyze the reaction.arrow_forward
- Allosteric activators block the active site, so the enzyme cannot bind True Or Falsearrow_forwardEnzymes are biological catalysts that fulfill the following general reaction mechanism: E+S [ES] [EP] E + P Where E is enzyme, S is substrate, and P is product. Briefly describe how an enzyme is able to speed of the rate of a reaction:arrow_forwardSince KM is an intrinsic property of an enzyme, its value does not depend on the enzyme concentration. True or Falsearrow_forward
- Define the following as they apply to an enzymatic reaction. Give an example of each. a. Enzyme-limited: b. Substrate-limited:arrow_forwardWould you expect an irreversible inhibitor of an enzyme to be bound by covalent or by noncovalent interactions? Why?arrow_forwardThe two types of enzyme activators are cofactors or coenzymes. True or falsearrow_forward
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