Consider the Michaelis-Menten enzymes below and answer the following questions.Kcat (s')9.5*105 1.4*10*2.5*102 1.0*1075.0*10 8.0*10²Enzyme Km (M)AВa. Which enzyme has the highest affinity substrate? How do you know?b. Which enzyme can convert the most substrate to product in a given period of time? Howdo you know?c. Which enzyme has the highest catalytic efficiency? How do you know?

Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

Answered: Consider the Michaelis-Menten enzymes…

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

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Similar questions

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Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the catalytic efficiency for this reaction. Report your answer in scientific notation to three significant figures in units of M-1s-1.
Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
The 2 eynzymes are affected by a substrate. Choose all correct answers.
Please atleast answer this question ?
For an experiment that tests the effect of enzyme concentration on catalase from Avocado activity( reaction rate), what materials would be needed?
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
An enzyme catalyzes the reaction M-N. The enzyme is present at a concentration of 0.0000000022 M, and the Vmax is 0.0000028 Ms1. The Km for substrate is 5.5 µM. Calculate kcat-
In an experiment, three batches of the same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor. In each batch, the inhibitor was of a different type: a.Batch 1: competitive inhibitor b.Batch 2:uncompetitive inhibitor c.Batch 3:non-competitive inhibitor Assuming that Vmax = 80 mM s', Km = 8 mM, and Kiof all three inhibitors was 10 mM, which of the inhibitors was the most efficient on Vo? Explain your answer.
1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?
Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.
Use the data from the table below to answer the questions on an ezyme obtained from potato extract. The greater the absorbance value, the more product generated for each chemical reaction Table 1: Summary Data for Enzyme Catalyzed Reaction Product Formation Measured as Absorbance Tube Distilled Water Catechol PTU (Inhibitor) Potato Extract Results (Absorbance) 1 5.5 ml 0.5 ml -- --- 0.02 2 5 ml 0.5 ml --- 0.5 ml 0.68 3 4.5 ml 0.5 ml 0.5 ml 0.5 ml 0.04 4 4.5 ml 0.5 ml 1.0 ml 1.26 5 4.5 ml 1.0 ml 0.5 ml 1.22 a) Explain with respect to enzyme activity why test tube 1 produced very little absorbance: b) Explain with respect to enzyme activity why test tube 3 produced very little absorbance: c) Explain how to tubes 4 and 5 differ with respect to reaction conditions. d) Explain with respect to enzyme activity why tubes 4 and 5 have similar absorbance and why both have…

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