Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
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Question
Chapter 19, Problem 19.54AP
Interpretation Introduction
Interpretation:
The rate of the reaction should be determined if the amount of an enzyme is tripled
Concept Introduction:
Enzyme:
- It is a protein or a molecule which can act as a catalyst for a biological reaction.
- Does not affect the equilibrium point of the reaction.
- Active site of the enzyme is the region where the reaction takes place.
- Enzyme’s activity can be specific which means the activity is limited to a certain substrate and a certain type of reaction and it is referred to as specificity of the enzyme.
- Decreases the time required for the reaction by lowering its activation energy.
Factors affecting enzyme activity:
Substrate concentration
Enzyme concentration
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Check out a sample textbook solutionStudents have asked these similar questions
In an enzyme-catalyzed reversible reaction
what happens when
a) rate of change of enzyme-substrate
complex concentration with time is positive
b) rate of change of enzyme-substrate
complex concentration with time is zero
9:0
A competitive inhibitor diminishes the rate of catalysis:
A) By reducing the proportion of enzyme molecules bound to a substrate.
OB) By altering the shape of the active site of the enzyme
C) By binding to a regulatory subunit
D) By enhancing the interaction between enzyme and reaction product
Why do we not determine the initial reaction rate when the enzyme is saturated with substrate?
Chapter 19 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 19.1 - Prob. 19.1PCh. 19.1 - The enzyme LDH converts lactate to pyruvate. In...Ch. 19.2 - The cofactors NAD+, Cu2+, Zn2+, coenzyme A, FAD,...Ch. 19.3 - Describe the reactions that you would expect these...Ch. 19.3 - Prob. 19.5PCh. 19.3 - Prob. 19.6PCh. 19.3 - Prob. 19.7PCh. 19.3 - Prob. 19.8PCh. 19.4 - Prob. 19.9KCPCh. 19.5 - Prob. 19.10KCP
Ch. 19.5 - Prob. 19.11PCh. 19.5 - Prob. 19.12PCh. 19.6 - Prob. 19.13PCh. 19.6 - Prob. 19.14PCh. 19.7 - (a) L-Threonine is converted to L-isoleucine in a...Ch. 19.8 - AZT (zidovudine) inhibits the synthesis of the HIV...Ch. 19.8 - Prob. 19.3CIAPCh. 19.8 - Prob. 19.16PCh. 19.9 - Does the enzyme described in each of the following...Ch. 19.9 - Prob. 19.18PCh. 19.9 - Compare the structures of vitamin A and vitamin C....Ch. 19.9 - Prob. 19.20PCh. 19.9 - Prob. 19.21KCPCh. 19.9 - Prob. 19.22PCh. 19.9 - Prob. 19.4CIAPCh. 19.9 - Prob. 19.6CIAPCh. 19.9 - Prob. 19.7CIAPCh. 19.9 - Enzyme levels in blood are often elevated in...Ch. 19.9 - Prob. 19.9CIAPCh. 19.9 - Prob. 19.23PCh. 19 - Prob. 19.24UKCCh. 19 - Prob. 19.25UKCCh. 19 - Prob. 19.26UKCCh. 19 - Prob. 19.27UKCCh. 19 - Prob. 19.28APCh. 19 - Explain how the following mechanisms regulate...Ch. 19 - Prob. 19.30APCh. 19 - Prob. 19.31APCh. 19 - Prob. 19.32APCh. 19 - Prob. 19.33APCh. 19 - Prob. 19.34APCh. 19 - Prob. 19.35APCh. 19 - Prob. 19.36APCh. 19 - Prob. 19.37APCh. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - What features of enzymes make them so specific in...Ch. 19 - Describe in general terms how enzymes act as...Ch. 19 - Prob. 19.42APCh. 19 - Prob. 19.43APCh. 19 - Prob. 19.44APCh. 19 - Prob. 19.45APCh. 19 - Prob. 19.46APCh. 19 - Prob. 19.47APCh. 19 - What is the difference between the lock-and-key...Ch. 19 - Why is the induced-fit model a more likely model...Ch. 19 - Prob. 19.50APCh. 19 - Prob. 19.51APCh. 19 - How do you explain the observation that pepsin, a...Ch. 19 - Prob. 19.53APCh. 19 - Prob. 19.54APCh. 19 - Prob. 19.55APCh. 19 - Prob. 19.56APCh. 19 - Prob. 19.57APCh. 19 - The text discusses three forms of enzyme...Ch. 19 - Prob. 19.59APCh. 19 - Prob. 19.60APCh. 19 - Prob. 19.62APCh. 19 - Prob. 19.63APCh. 19 - The meat tenderizer used in cooking is primarily...Ch. 19 - Prob. 19.65APCh. 19 - Why do allosteric enzymes have two types of...Ch. 19 - Prob. 19.67APCh. 19 - Prob. 19.68APCh. 19 - Prob. 19.69APCh. 19 - Prob. 19.70APCh. 19 - Prob. 19.71APCh. 19 - Prob. 19.72APCh. 19 - Prob. 19.73APCh. 19 - Prob. 19.74APCh. 19 - Prob. 19.75APCh. 19 - Prob. 19.76APCh. 19 - Prob. 19.77APCh. 19 - Prob. 19.78APCh. 19 - Prob. 19.79APCh. 19 - Prob. 19.80CPCh. 19 - Prob. 19.81CPCh. 19 - Prob. 19.82CPCh. 19 - Prob. 19.83CPCh. 19 - Prob. 19.84CPCh. 19 - Prob. 19.85CPCh. 19 - Prob. 19.86CPCh. 19 - Prob. 19.87CPCh. 19 - Prob. 19.88GPCh. 19 - The ability to change a selected amino acid...Ch. 19 - Prob. 19.90GPCh. 19 - Prob. 19.91GP
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- What does an enzyme change relative to an uncatalyzed reaction? a) The rate of the reaction. b) The free energy change of the reaction. c) The size of the active site. d) The pH. e) The equilibrium constant.arrow_forwardMULTIPLE CHOICE Compared to an uncatalyzed reaction, an enzyme-catalyzed reaction ________. A) uses less substrate B) produces different products C) occurs at a faster rate D) requires more energy E) requires a higher temperaturearrow_forwarda) What is the Steady State assumption; how does steady state differ from equilibrium? b) Transition state; what are two ways that enzymes can decrease the transition state energy?arrow_forward
- b) Enzymes accelerate reactions by facilitating the formation of the transition state. Define transition state and activation energy. For full credit, you need to present the actual graph (for an endergonic or exergonic reaction - make sure to specify your choice) highlighting each term? c) Explain how an irreversible inhibitor for an enzymatic reaction differs from reversible inhibitors. Provide specific example of an irreversible inhibitor and its target enzyme d) Determine the Vo as a function of Vmax when the substrate concentration is equal to 10 KM or 20 KM. What does this tell you about an enzyme ability to reach Vmax?arrow_forwardWhen studying the mechanism of the enzymatic reaction, functional groups were found that ensure the connection of the enzyme molecule with the substrate and take a direct part in the act of catalysis. What are these areas of the enzyme formed by these groups called? What functional structures form them and why?arrow_forwardWhat class of enzyme catalyzes the following?arrow_forward
- The active site of an enzyme is usually a groove or pocket on the surface that A) binds allosteric regulators of the enzyme. B) is involved in the catalytic reaction of the enzyme. C) is inhibited by the presence of a coenzyme or a cofactor.arrow_forwardIn a typical enzyme-catalyzed reaction, what are the relative concentrations of reactants and products as compared to the enzyme concentration?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
- One 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_forwardgive the properties of the enzyme (e.g., shape, size, colour, price). a) amylase b) invertasearrow_forwardChoose the best answer The active site of an enzyme is the place where the following happens: a)The enzyme-substrate complex forms and the reaction occurs at the active site. b)The enzyme substrate complex forms here. c)The catalytic reaction happens here. d)Allosteric regulation of enzyme rate occurs here. e)All of these are correct.arrow_forward
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