61. MATHEMATICAL For the following aspartase reaction (see Ques-tion 28) in the presence of the inhibitor hydroxymethylaspar-tate, determine K and whether the inhibition is competitive ornoncompetitive.[S](molarity)V, No Inhibitor(arbitrary units)V, Inhibitor Present(same arbitrary units):21×10¹01 0.026 TOIV 0.0109 95 X 100.0920.0400.0860.12010-3IPO?2.5 10-³5×10 211 0.150 09Mein5 X 10-30.16520 mys0.142

Assuming the enzyme follows Michelis Menton's enzyme Kinetics. The initial velocity of the enzymatic…

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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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Kinetic Parameters of Enzyme-Catalyzed Reactions TABLE 12-1 The Values of KM, Keat, and Keat/KM for Some Enzymes and Substrates Enzyme Substrate KM (M) 9.5 x 10-5 1.2 x 10-² 2.6 x 10-2 2.5 x 10-2 4.4 x 10-1 8.8 x 10-2 6.6 x 10-4 Acetylcholinesterase Carbonic anhydrase Catalase Chymotrypsin Fumarase Urease Acetylcholine CO₂ HCO₁ H₂O₂ N-Acetylglycine ethyl ester N-Acetylvaline ethyl ester N-Acetyltyrosine ethyl ester Fumarate Malate Urea 5.0 x 10-6 2.5 x 10-5 2.5 x 10-2 Keat (S-¹) 1.4 x 104 1.0 × 106 4.0 × 105 1.0 X 107 5.1 x 10-2 1.7 × 10-1 1.9 X 10² 8.0 x 10² 9.0 × 10² 1.0 X 104 Keat/KM (M¹s¹) 1.5 × 108 8.3 x 107 1.5 x 107 4.0 X 108 1.2 x 10-1 1.9 2.9 × 105 1.6 × 108 3.6 X 107 4.0 X 105 Which enzyme is the most catalytically efficient? Which substrate does chymotrypsin bind to most tightly (assume k_₁ >> K₂)? Is fumarate or malate a better substrate of fumarase? Is it possible to have a kcat/KM of greater than 1 x 10⁹ M-¹ s-¹? Why or why not?
Activity, Enzyme Kinetics Biol 250, Spring 2022 The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are as follows: [S] (umol/L) V [(µmol/L) min1] 5 22 10 39 20 65 50 102 100 120 200 135 (a) Estimate Vmax and KM from a direct graph of v versus [S]. Do you find difficulties in getting clear answers? (b) Now use a Lineweaver-Burk plot to analyze the same data. Does this work better? (c) Finally, try an Eadie-Hofstee plot of the same data. (d) If the total enzyme concentration was 1 nmol/L, how many molecules of substrate can a molecule of enzyme process in each minute? (e) Calculate kcat/KM for the enzyme reaction. Is this a fairly efficient enzyme?
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Transformation of pGLO in E. coli: 8) Explain your expected results on LB, LB+Amp, and LB+Amp+Arabinose plates for the -pGLO and the +pGLO treatments. (6 total results, please assume everything works) Please describe how much growth, and whether if will or won’t glow.
Enzyme Kinetics question Enzyme used is 10uL of a 10 ng/uL solution to a reaction mix in a final volume of 2.0 mL. (Enzyme used is 20kDa monomeric enzyme if matters) Based off lineweaver burk where 300 uM of inhibitor is used noninhibited formula is y= 4x + 0.1 (x axis is 1/S 1/mM) (y axis is 1/Vo sec/mM) inhibited formula is y = 4x + 1 I found Km as 1 mM for inhibited Vmax as 1mM/sec for inhibited How would I find Kcat? How would I find Ki?
Processing of results Calculate (and show your calculations) for each acetic acid solution 1. the molar conductivity, Am (S m² mol¹), 2 the degree of ionisation, a 3. the ionisation constant, Ka 4. [H3O] = αcм and the pH = -log [H3O+]. Finally, calculate an average value for the ionisation konstant, Ka, of acetic acid with its standard deviation. Compare your result with a literature value and make a statement whether it is significantly different or not.
In response to epinephrine for the "fight or flight" response, there is INCREASED activity of PEP carboxykinase in the liver. What is the function of PEP carboxykinase? Enter your answer here Why is it beneficial to increase the activity of PEP carboxykinase in the liver in response to epinephrine for the "fight or flight" response? Enter your answer here
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