Below is data collected from an experiment that examined the activity of Enzyme A at three different temperatures. The amount of product formation was measured in mg/min. Cold Enzyme Room Temp Enzyme Boiled Enzyme 3 mg/min 10 mg/min Amg/min Based on the above results: What is the optimal environment for this enzyme? Describe in detail what most likely happened to the enzyme in the boiled temperature.

Below is data collected from an experiment that examined the activity of Enzyme A at three different temperatures. The amount of product formation was measured in mg/min. Cold Enzyme Room Temp Enzyme Boiled Enzyme 3 mg/min 10 mg/min Amg/min Based on the above results: What is the optimal environment for this enzyme? Describe in detail what most likely happened to the enzyme in the boiled temperature.

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

See similar textbooks

Similar questions

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.
Most of the enzyme reactions followed the mathematical kinetic plots suggested by the Michaelis-Menten plots:viii. Draw another Lineweaver-Burk plot and on the same plot, draw a graphto indicate un-competitive inhibition.Note: In the graphs, lable Vmax and KM clearly.
When reviewing a Michaelis-Menten Saturation Curve, at first the rate of the reaction is relatively constant, but the rate decreases as the substrate is used up and eventually reaches a plateau. Afte reaching this plateau, what would speed up the reaction again? Adding more substrate Adding heat Adding more enzyme Adding cofactors
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.
assume that for an enzyme immobilized on the surface of a nonporous support material, the external mass-transfer resisitance for substrate is not negligible as compared to the reaction rate.The enzyme is subject to substrate inhibition are multiple states possible?why or why not? could the effectiveness factor be greater than one?
What is the initial velocity measurement for the hydrolysis of 50 μM amoxicillin by the enzyme?
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-
None
Using the table below can you please help me answer the following. Based on your results, what can you conclude about the effect of enzyme concentration on reaction rate? Explain
You run a series of assays at 25°C on enzyme A. You measure the velocity for a range of S concentrations. What is the Km (in mM) for Enzyme A?
You measure the kinetics of an enzyme as a function of substrate concentration using the Lineweaver-Burke equation. The enzyme concentration is maintained constant at a level of 1 μM. From these data, determine the equation of the line, Vmax, KM, and kcat for the enzyme. [S], μM Velocity, μM/min 2 2.9 3 3.8 4 4.4 5 5.0 6 5.4 7 5.8 8 6.2 9 6.4 10 6.7 The Lineweaver-Burke equation is 1V=1V= ____________(1[S])(1[S]) + ___________. Therefore, the Vmax is ____________ μM/min, KM is ____________ μM, and kcat is ____________ /min. Round-off all answers to four (4) decimal places.