please draw the whole mechanism.Thank youงс16. Draw out a reaction mechanism for phosphorylation of a tyrosine hydroxyl group. Your mechanism shouldshow how the phosphonyl in ATP has carbonyl-like character. For this mechanism, you need to draw thestructures of tyrosine and ATP. Make sure to regenerate the enzyme in its resting form. (6 pts.)KinaseProtein OH +ATPProtein-O+ADP

Mechanism:Nucleophilic Attack: The hydroxyl group on serine acts as a nucleophile and attacks the…

Answered: please draw the whole mechanism. Thank…

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter6: An Overview Of Organic Reactions

Section6.SE: Something Extra

Problem 18VC: Look at the following energy diagram for an enzyme-catalyzed reaction: (a) How many steps are...

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Free Energy A+B a. Progress of the Reaction C. d. e. C+D A. Is the above reaction endergonic or exergonic? B. Which letter is AG of the reaction? C. Which letter is the activation energy of the enzyme catalyzed reaction? D. Which letter is the activation energy of the original reaction? E. If the above reaction has a AG of -3.6 kcal/mol could it be coupled to power kcal/mol?
An enzymatic assay was performed using the enzyme phophofructokinase-1, which catalyses the committed step of the glycolysis pathway. What is the final concentration of the fructose 6-phosphate substrate in a test tube containing the following: 250 µL of 150pM fructose 6-phophate, 100 µL 20 mg.ml-1 phosphofructoskinase-1 and 150 µL 100mM buffer pH 7.5
Trypsin is a serine protease that has a KM of 15 mM. At an initial substrate concentration of 250 µM insulin, trypsin is found to degrade insulin at a rate of 0.6 µM/min. If the concentration of trypsin in solution was 4.326 µM, what is the kcat of trypsin in s-1?
Draw a carboxylic acid that results from the hydrolysis of glyceryl tributyrate. Include only one carboxylic avid product in your answer.
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Consider the molecular structure of a disaccharide. OH OH HO ©Macmillan Learning I H OH I I- I H I OH H HO OH OH H OH Identify the type of glycosidic linkage in the disaccharide. ○ẞ (12) Oẞ (14) a (12) (+11) 10 Label the structures to show the monosaccharide units produced by hydrolysis of the disaccharide. O Answer Bank H CH₂OH OH -0. C
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Problem 1. At the given temperature, experimental data for enzyme-catalyzed reaction rates were obtained as follows. Answer the following questions. The initially added enzyme concentration, [E.], was 2 mol/L. The reaction rates in the absence and the presence of an inhibitor were measured. The concentration of the inhibitor was 0.5 mol/L. [S] (mol/L) v (no inhibitor) (mol/L-min) v (inhibitor presence) (mol/L.min) 0.1 3.7 0.05 3.0 0.03 2.5 0.015 1.8 0.005 0.7 1.3 1.2 1.1 0.9 0.5 a. Calculate the values of Km and Vm in the absence of the inhibitor. b. Calculate the value of K₁ in the presence of the inhibitor. c. Draw the catalytic mechanism of the reaction in the presence of the inhibitor. d. Identify the type of inhibitor.
Express the initial velocity of α-amylase in terms of substrate disappearance and product (as glucose) formation.
(10 pts) What is the free energy of hydrolysis of glycylglycine at 37°C and 1 bar? aA H and AS are independent of r r the temperature range. bA H is independent of the r temperature range, but A Sis r dependent on temperature. Hint: find AG at 25°C first. r (10 pts) What is the free energy of hydrolysis of glycylglycine at 37°C and 1 bar? H₂N зая Glycylglycine OH +H₂O 2 H₂Ni OH Glycine a) Assume that both A.H and A.S are independent of the temperature range. b) Assume that A,H is independent of the temperature range, but AS is dependent on temperature. Hint: find A.G at 25 °C first.

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