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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Chapter 19.5, Problem 19.10KCP
Interpretation Introduction
Interpretation:
The meaning of the state at which an enzyme is saturated with the substrate should be identified and also the effect on the rate of the reaction on adding more substrate and more enzymes should be given.
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
Expert Solution & Answer
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Check out a sample textbook solutionStudents have asked these similar questions
An enzyme has a single active site at which it can bind and hydrolyze either
X or Y; however, the enzyme cannot bind X and Y at the same time. Answer
the following questions regarding the Km and Vmax of this enzyme.
(a) Will the Km for X be affected if Y is present in the reaction mixture?
Explain.
(b) Will Vmax for X be affected if Y is present in the reaction mixture? Explain.
(a) No, X competes with Y for binding, so the apparent Km for X
will stay the same.
(b) Yes, the Vmax for X will decrease in the presence of Y.
(a) No, Y does not compete with X for binding, so the apparent Km for X
will stay the same.
(b) No, the Vmax for X will be unaffected by the presence of Y.
The total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S]
Explain why [S] >> [ES]
Hence explain why [Sf] ~ [S]
Which of the following is TRUE under the following conditions: the enzyme
concentration is 2.5 nM, substrate concentration is 75 nM, the KM = 150 nM, and
the Vmax = 20 nmol/min
a) The rate of the reaction is 20 nmol/min!
b) The rate of the reaction is between 10 nmol/min and 20 nmol/min.
c) The rate of the reaction is 10 nmol/min.
d) The rate of the reaction is below 10 nmol/min.
e) The rate cannot be determined from the above information.
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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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Given: Your professor gives you a vial of enzyme and a vial of substrate. The product of this reaction is fluorescent and you can measure the concentration of the product as a function of time. (answer a, b, and c)a) Your professor tells you to quantify how much product is being produced per minute at thebeginning of the experiment. What exactly are you measuring?b) On the same plot, show the kinetic curve for an increased quantity of enzyme. Assume a 2x concentration. Indicate Km and Vmax.c) You don’t have a computer hand. Sad. How can you plot the data such that you can get important Michaelis-Menten values?arrow_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_forwardThe total concentration of enzyme in a reaction, [E], is made up of the concentration of enzyme bound to substrate, [ES], and the concentration of enzyme still free in solution, [Ef]. Similarly, the total amount of substrate is made up of [Sf] and [ES]. We can assume that the concentration of enzyme is much less than that of the substrate, [E] << [S]. Assuming the steady state condition and the relationships between [E], [Ef] and [ES], and similar ones for S, given in lectures, derive an expression for the saturation factor, , in terms of [S] and . (Note that [E] and [S] denote the total amounts of enzyme and substrate added to the reaction, respectively. You may assume that [S]>>[E].)arrow_forward
- What is the defining characteristic for an enzyme catalyzing a sequential reaction? A doubledisplacement reaction?arrow_forwardWhat is the difference between enzyme limited and a substrate limited reaction?arrow_forwardWhich of the following would best explain how an enzyme catalyzes two different reactions? A) The enzyme contains a-helices and B-pleated sheets. B) The enzyme is subject to cooperativity C) Either the enzyme has two distinct active sites or the substrates involved in the two reactions have very similar structures D) The enzyme is subject to competitive inhibition and allosteric regulation E) The enzyme is composed of at least two subunitsarrow_forward
- 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 9:0arrow_forwardgive the properties of the enzyme (e.g., shape, size, colour, price). a) amylase b) invertasearrow_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_forward
- The figure below represents a reaction in the presence and absence of an enzyme catalyst. What can you conclude about this reaction? energy activation energy activation energy 1 uncatalysed reaction catalysed reaction A) It is endergonic in the absence of the enzyme. B) It will proceed more quickly in the presence of the enzyme. C) Once the reaction has reached equilibrium, there will be more product in the enzyme-catalyzed reaction. D) It has a negative AG. OE) Both B and D are truearrow_forwardA 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 productarrow_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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