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.
Ll.83.
What is the correct answer?
Express the initial velocity of α-amylase in terms of substrate disappearance and product (as glucose) formation.
Enzyme X can act on either substrate A or B; the Km on A < Km on B. Vmax for A > Vmax on B.Sketch 1 plot for 1/v vs. 1/[S] plot for Enzyme X in the presence of A and in the presence of B.
The students were given a compound X. They are told that it inhibits LDH activity. The studentsdecided to check that by including it in the assay and testing the effect of the inhibitor using variousconcentrations of substrate (pyruvate), in the presence of NADH. They evaluated the rates of theLDH reaction with and without the inhibitor compound. Data obtained are shown below. [pyruvate] mM Reaction rate without compound X 10-9moles per second Reaction rate with compound X (10-9moles per second) 1 2.04 1.18 2 2.86 2.0 4 3.70 2.8 8 4.35 3.6 12 4.76 4.0 1(a). Estimate Vmax and Km for LDH with and without the inhibitor. 1(b). Determine the type of inhibition of the enzymatic reaction from the data the students collected in the presence and absence of the inhibitor X. 1(c). Students were told that compound X is N-propyl oxamate. The structures of pyruvate and N-propyl oxamate are shown below. Is the information shown below consistent…
I realllyyy need help with this one please help
Oxaloacetate is an inhibitor of succinate dehydrogenase because it is structurally very similar to succinate as shown below. Also, its binding to the enzyme does not involve any covalent bond formation. What type of inhibitor is oxaloacetate? COO | CH₂ 1 CH₂ 1 COO Succinate COO | CH₂ C=O COO Oxaloacetate O a noncompetitive inhibitor both a noncompetitive and an irreversible inhibitor O an irreversible inhibitor O a competitive inhibitor
Acetolactate synthase transfers the acyl group of pyruvate to alpha-ketobutyrate. This is the first step in the biosynthesis of the amino acid isoleucine. Propose a mechanism for this reaction.

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