15. Dodgerase is an enzyme that is exquisitely inhibited by a class of cheaters(Astrozolamide and Redsoxin). Dodgerase plays an important role in the civic pride ofone of the greatest and most diverse cities in the world. The experimental curve ofinitial reaction velocity (as percentage of Vmax) versus [S] for the Dodgerase reaction isshown (upper curve). When the experiment was run in 2017, in the presence ofinhibitor, the lower curve was obtained. From an inspection of the curves and yourknowledge of the kinetic properties of competitive, uncompetitive and mixed inhibitors,determine the nature of the inhibition by Astrozolamide and explain your reasoning!100No inhibitor50Astrozolamide0.20.40.60.8[S] (mm)pee"A JO %) A

Enzymes are globular protein molecules that catalyze a given reaction in a time-dependent manner.…

knowledge of the kinetic properties of competitive, uncompetitive and mixed inhibitors, determine the nature of the inhibition by Astrozolamide and explain your reasoning! 100 No inhibitor Astrozolamide 0.2 0.4 0.6 0.8 (S) (mm) pre"A JO %) A

knowledge of the kinetic properties of competitive, uncompetitive and mixed inhibitors, determine the nature of the inhibition by Astrozolamide and explain your reasoning! 100 No inhibitor Astrozolamide 0.2 0.4 0.6 0.8 (S) (mm) pre"A JO %) A

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Related questions

Q: ENZYME KINETICS ANALYSIS Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric…

A: Enzyme kinetic: [S]is the concentration of substrate V is the velocity The Lineweaver-Burk plot of…

Q: Show how the addition of a competitive inhibitor would affect the reaction velocity and…

A: Enzymes are high molecular weight proteins that catalyse biochemical reactions. They contain an…

Q: Zinc is an important inorganic mineral in our diets. Zinc ions (Zn) need to be present in certain…

A: Several physiological functions of the human body depend on zinc, an important element. Carbonic…

Q: An inhibitor has a K, of 0.1 µM in its interaction with an enzyme. What then are the Ka and Ka…

A: An enzyme is a protein molecule that increases the rate of the reaction by decreasing the activation…

Q: Drug Metabolism Reactions Identify the enzyme family involved in the following metabolic reaction:…

A: Drug metabolism is the process in which a substance of therapeutic nature is converted to some other…

Q: 6. Noncompetitive inhibition is a limiting case in which the effect of binding inhibitóf has no…

A: Non-competitive inhibitors binds to both enzyme-substrate complex, and enzyme only. Also, substrate…

Q: Q7. Kinetics were analysed for an enzyme in the absence and presence of inhibitor. In the absence of…

A: In competitive inhibition the inhibitor competes with substrate for binding to an active site. In…

Q: Aldolase enzymes have the following rate constants. k₁ = 10³M ¹s¹, k-₁ = 4.4x10 s ¹, k₂ = 10's-¹ -1…

A: Consider the following single substrate (S) enzyme (E) catalyzed reaction mechanism given below E +…

Q: .Hanes-Woolf 2.Michaelis Menten 3.Lineweaver-Burk limitations: A. This plot appears to allow for…

A: For enzymes that follow Michaelis Menten-type kinetics, the determination of accurate values of Km…

Q: I want to solve the last 2 sub-parts

A: Kcat is the enzyme turnover number. It is the number of molecules of substrate that an enzyme…

Q: How much transformed free energy would be required to provide cells with 7.8 mM ATP at 37 °C if both…

A: The standard free energy change (∆G°') for the hydrolysis of ATP to ADP and inorganic phosphate (Pi)…

Q: A. Effect of Enzyme Concentration Table 1. Effect of Catalase Concentration on Enzyme Activity…

A: "Since you have posted multiple questions, we will provide the solution only to the first question…

Q: The ideal temperature for an enzyme, Enzyme A, is 34.5 degrees Celsius. Km = 15.0 M, Vmax = 12.0 M/s…

A: Enzymes are biocatalysts which increase the rate of biochemical reactions. Enzymes will not catalyze…

Q: estions The enzyme maltase combines the substrates Starch molecule to produce the disaccharide…

A: Proteins that act as biological catalysts are enzymes. Chemical reactions are accelerated by…

Q: An enzyme catalyzes He veaction AZB, The en&yme is present at a Cencentration of 2nl, an Vmax s 22…

A: A study that deals with the reaction (conversion of substrate into the product) catalyzed by enzymes…

Q: 1/V sec/mM -6-4-2 1.0 0.8 0.6 0.4 0.2 2 4 A B 6 8 10 1/[S] MM-1 inhibited enzyme uninhibited enzyme…

A: For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…

Q: in the presence of a noncompetitive inhibitor 24) Relation between Reaction Velocity and Substrate…

Q: Energy Conversion Problem 1. a) Influence of concentration on the free energy change. In frog…

A: For the chemical reaction:aA + bB -> cC + dDThe reaction quotient Q is calculated as:Q = ([C]^c *…

Q: For the reaction glutamate (aq) + oxaloacetate²- (aq) a-ketoglutarate2- (aq) + aspartate¯ (aq) the…

A: Standards free energy change calculated at biochemical standards is called biochemical standard free…

Q: 16) The graph at right shows the results of reaction rate vs. substrate concentration for a…

A: Since you have posted multiple questions we will answer the first question for you. If you want any…

Q: Q14) Exercise 3 on the following pages is referring to a disputed 2010 study claiming that bacteria…

A: there are some points related to DNA and kinetics Which are as follows: As we know basically…

Q: 2. Peter does not tolerate lactose in milk. He bought a solution of ß-galactosidase where [Eo] 10.0…

A: First lets find the Vmax value of the enzyme β-galactosidase. Vmax = Kcat×Etotal =525 s-1…

Q: 2. The kinetics of an enzyme are measured as a function of substrate concentration in the presence…

A: Enzymes are catalysts that increase the rate of biochemical reactions. The inhibition of enzyme…

Q: The Lineweaver-Burk plots in this figure represent the activities of enzymes in the absence and…

A: Inhibition : Compound which converts the enzyme into inactive substance and adversly effect the rate…

Q: Enzymes work fastest at the start of a process and this is called (1). As the enzyme concentration…

A: The enzymes are the biocatalyst that speed up a biochemical reaction. At the end of the chemical…

Q: .) Match the statement with the enzyme. Each blank may have one or more enzymes or none (leave…

A: Lactate dehydrogenase carries out interconversion of pyruvate and lactate along with NADH and NAD+.…

Q: 3. Show how the addition of an uncompetitive inhibitor would affect the reaction velocity and…

A: Enzymes are high molecular weight protein that catalyse biochemical reactions. They contain a active…

Q: Determine Km and Vmax using Lineweaver-Burke in the presence and absence of inhibitor. What type of…

A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…

Q: 66 a only

Q: Problem 2 The fundamental mechanism of many drugs is their ability to inhibit certain enzymes. One…

A: Enzyme kinetic parameters are Km and Vmax. Km is called michaelis menton constant which is nothing…

Q: How is genetic engineering beneficial to plants and animals?

A: Genetic engineering is defined as the processes or techniques required for the alteration of genetic…

Q: Specificity Constant Turnover number Michaelis Constant Maximum Velocity 2. [] 3. s1 4. [11.51 5. S…

A: The specificity constant, denoted by kcat/Km, is a measure of how efficiently an enzyme converts…

Q: In Michaelis menton kinetics which variable is held constant? multiselect a. substrate concentration…

A: Hi! Thank you for the questions. As you have posted multiple questions, I will be answering the…

Q: blem asks students to think about enzyme kinetics in the framework of the Michaelis-Menten equation.…

A: X-axis: Concentration of CO2 (µM to mM)Y-axis: Amount of HCO3 produced (arbitrary units)

Q: 100 increasing enzyme ativity 50 optimum pH 5 6 7 9 10 11 8 pH 20 40 Temperature 1. How do pH and…

A: Every enzyme exhibits maximum activity over the certain pH range in which a molecule exists in its…

Q: 3. For clopidogrel, draw the structure of clopidogreli and label the structure with its indication…

A: Clopidogrel is a pro drug that upon activation by the liver enzymes becomes an active metabolite.…

Q: 5. Please draw typical curves of the relationship between enzyme catalytic rate(v)and substrate…

A: Enzymes are proteins that catalyze biochemical reactions. Catalytic activity refers to the rate at…

Q: The effect of an inhibitor on an enzyme was tested and the experiment gave the results below. If…

A: Inhibition can be either reversible or irreversible. Reversible inhibition can be generally of 3…

Q: För an enzyme that displays Michaelis-Menten kinetics, the Vmax is 0.06 M/min at 0.8 M (enzymes…

A: Given, Vmax = 0.06 M/min at Substrate concentration , [S] = 0.8 M At Substrate concentration [S] =…

Question

15. Dodgerase is an enzyme that is exquisitely inhibited by a class of cheaters
(Astrozolamide and Redsoxin). Dodgerase plays an important role in the civic pride of
one of the greatest and most diverse cities in the world. The experimental curve of
initial reaction velocity (as percentage of Vmax) versus [S] for the Dodgerase reaction is
shown (upper curve). When the experiment was run in 2017, in the presence of
inhibitor, the lower curve was obtained. From an inspection of the curves and your
knowledge of the kinetic properties of competitive, uncompetitive and mixed inhibitors,
determine the nature of the inhibition by Astrozolamide and explain your reasoning!
100
No inhibitor
50
Astrozolamide
0.2
0.4
0.6
0.8
[S] (mm)
pee"A JO %) A

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

SEE SOLUTION Check out a sample Q&A here

Step 1Introduction

VIEW

Step 2 Inhibitors

VIEW

Step 3 According to question,

VIEW

Step by step

Solved in 3 steps

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

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

Please do all the questions
31
33..
Can I get help with these two questions?
Comparison between simple enzymes and complex enzymes. In the table are the characteristics for comparison. I guessed a few of them (added a check mark)
Pls help ASAP. Pls I humbly request to do both questions.
4
Need help on all parts and explanation
Case Study: Enzyme Kinetics Data for new statin drug (inhibits HMG CoA reductase): ● ● I Substrate (UM) 0.5 1.0 1.5 2.5 3.5 || Rate of reaction (mm/min) 23.5 32.2 36.9 41.8 44 What are the Kms of the uninhibited and inhibited reactions? Rate of reaction in presence of 5.0 nM statin Using the above date, create a double-reciprocal (Lineweaver Burk) plot. What type of inhibition is shown by the new statin? What are the Vmax of the uninhibited and inhibited reactions? 16.67 25.25 30.49 37.04 38.91
Please explain your reasoning for every answer
please help me identify these huhu thank you
Match with the given reaction A. The reaction with a non-competitive inhibitorB. The reaction without inhibitorC. The reaction with competitive inhibitorD. The reaction with the fastest reaction