3.Rennin is an enzyme that follows the following reaction mechanism:S+E <==1==> ES ==2==> P + EThe first reaction has kinetic constants k₁ and k₁, while k₂ is the rate constant for the second reaction.A. Look up rennin and classify it as one of the 6 types of enzymes discussed in class.B. Give an example of a substrate used with rennin, and what product/type of product results in industry.C. Given values for the kinetic constants:k₁ = 1.75 * 10 L/mol-sk.₁ = 2.66 * 104 s.¹K₂ = 9.53 * 10³ S-¹What is the Michaelis Constant for this enzyme if you use the Rapid Equilibrium, RE, Assumption?What is the Michaelis Constant for this enzyme if you use the Quasi Steady State Assumption, QSSA?(Note: we found the relationship between the kinetic constants and Km and Vmax in class for this mechanism using bothapproaches}D. Using the values in (C), for a rennin concentration of 1.27* 105 M, and the Michaelis-Menten equation withKm values from part C, determine the initial reaction velocities (for both RE and QSSA) when thesubstrate is at a concentration of 4.88 x 10-³ M?(Note: both RE and QSSA will predict the same maximum reaction velocity, Vmax, for THIS mechanism}

Enzymes are generally divided into 6 main classes. The 6 main classes are; Oxidoreductases…

Answered: 3. Rennin is an enzyme that follows the…

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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1.The diagram below shows an outline of the aminotransferase mechanism that skips the specific steps that show how electrons flow when a Schiff base is formed or is hydrolyzed. Using the mechanistic details given below A. Draw the mechanism for Enzyme- PLP Schiff base formation using pyridoxal and the lysine amine group using arrow to indicate electron flow. B. Draw the mechanism for hydrolysis of the Schiff base to form the a-keto acid, which is the reverse of the first reaction. Stage 1 Lys residue 2-O,PO- Enz Amino acid Lys residue (CH2)4 (CH₂2)4 H R-C-COO R- NH₂ NH₂ R-C-COO *NH₂ H H- 2-0,PO- 2-0,PO- A. show how this forms Stage 1 Lys residue Enz (CH2)4 HO 2-O,PO Enzyme-PLP Schiff base OH Amino acid-PLP Schiff base (aldimine) LOH 2-0₂PO- OH 20,PO- a-Keto acid COO Ketimine a-Keto acid 2-0,PO- R-C- NH₂ B. show how the a-keto acid forms a-Keto acid H Enzyme-PLP Schiff base الرواية وطري Ketimine Pyridoxine (vitamin B6) Pyridoxal phosphate (PLP) Pyridoxamine phosphate Stage 2 Amino acid…
1. Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis? 2. Some plants contain compounds that inhibit serine proteases. It has been hypothesized that these compounds protect the plant from proteolytic enzymes of insects and microorganisms that would damage the plant. Tofu, or bean curd, possesses these compounds. Manufacturers of tofu treat it to eliminate serine protease inhibitors. Why is this treatment necessary?
Match the following catalytic strategies with their example. Place a Letter on the picture. There are only two examples given. CH2OH CH2OH H. CH,OH CH2OH он он OH Kon + H2O OH HO OH OH OH HO но OH OH OH OH A. Oxidoreducatase OH OH B. Transferase C. Hydrolase D. Lyase NH3 E. Isomerase F. Ligase R-CH-COO + 00C-CH2-CH2-C-COO Amino acid a-Ketoglutarate NH3 + 00c-CH2-CH2–CH-C0 R-C-COO a-Keto acid Glutamate
7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 Rate constants (k's) for the reverse reactions are: k-1, k-3, K.4, k.6, and k.7 Write the enzyme balance for this mechanism. How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)
Rearrange the following terms to show the process of enzymatic reaction. Use and + to complete the equation. enzyme enzyme-substrate complex enzyme product substrate Several important things should be noted about this reaction: 1. A/an because of the fit between their structures; 2. As a result, something happens to the example, it might be split in two at a particular location. 3. Then the and 4. The enzyme is again. 5. Note that the arrows in the formula for enzyme reaction point acts on a specific to form a/an molecule. For comes apart, yielding the in the reaction and is now free to react _- This means that the reaction is 6. An enzyme-substrate complex can simply go back to the the 7. The products of an enzymatic reaction can react with the enzyme to form the and again; 8. It, in turn, may again form the 9. Therefore, the same. and the may act to cause a to go either way.
1/Vo 1/[S] with I without I with I with I 1/vo without I *-*- 1/vo without I 1/[S] 1/[S] 3. The above graphs are lineweaver-burk plots that demonstrate how inhibitors affect Michaelis Menten enzymes. For each graph identify the type of inhibition and explain how you determined that this enzyme is kinetically demonstrating this type of inhibition.
Lysozyme catalyzes a "bi-bi" reaction, which means there are (how many) reactants and (how many) products. List, in order, the reactants that bind and the products that are released during a lysozyme-catalyzed reaction cycle -- be succinct but be specific. 1. First reactant = 2. First product = 3. Second reactant = 4. Second product %3D
A7. Consider what can be concluded about the catalytic site (substrate binding site) of phosphatase and the binding site of NaF from the type of inhibition shown by NaF for phosphatase and illustrate it schematically. The inhibition typre is pure noncompetitive inhibition.
Match the following catalytic strategies with their example. Place a Letter on the picture. There are only two examples given. CH2OH CH2OH CH2OH CH2OH он он OH OH + H20 OH OH OH но H. но но OH OH OH OH OH OH A. Oxidoreducatase B. Transferase C. Hydrolase D. Lyase NH3 E. Isomerase F. Ligase R-CH-COO "ooc-CH2-CH2-C-COO Amino acid a-Ketoglutarate
24. Consider the figure below, which is an alternate way to depict the energy changes occurring during a reaction from Substrate (S) to Product (P), when uncatalyzed (curve A) and when catalyzed by an enzyme (curve B). Note that curve B is not the same way we modeled an enzyme-catalyzed reaction in class; this model is a different, perhaps slightly more realistic, way of conceptualizing the energy changes over the course of a reaction than what we did in class. S and ES represent the transition states for reaction of the free substrate (S) or the enzyme-substrate complex (ES). T T activation energy for uncatalyzed reaction EST S edhosob nohtum od bluo woH abiow yedio 2 wwolaixa-y odi no vaigin oroda dapng odt ni o nfog) r gibadhoa P B ES EP progress of reaction activation energy for catalyzed reaction a) Explain briefly why, in curve B, the energy state of the enzyme-substrate complex is less than the energy state of the substrate alone. b) Suppose the enzyme in the diagram was mutated…
What type of inhibition is observed from the shift of the Lineweaver-Burke plot ahown in the graph below where the solid Ine represents the uninhibited enzymatic reaction while the broken line represents the inhibited enzymatic reaction? A. Irreveraible inhíbítion B. Noncompetitive inhíbition C. Competitive inhíbition D. Uncompetitive inhibition Potassium cyanide ia a polson which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with respect to reduced cytochrome c. Which type of inhibition does this represent? A. Irreveraible inhibition c. Competitive inhibition D. Uncompetitive inhibition B. Noncompetitive inhibition _10. Which of the following enzyme classes catalyze reactions in which two molecules become dissociated from each other? A. Kinase в. Нуdrolase c. Isomerase D. Ligase Which of the following enzyme classes catalyze reactions in which two molecules become covalently linked to each other? A. Kinase B. Hydrolase…
A hypothetical three-step metabolic pathway consists of intermediates W, X, Y, and Z and enzymes A, B, and C. Deduce the order of the enzymatic steps in the pathway from the following information: 1. Compound Q, a metabolic inhibitor of enzyme B, causes Z to build up. 2. A mutant in enzyme C requires Y for growth. 3. An inhibitor of enzyme A causes W, Y, and Z to accumulate. 4. Compound P, a metabolic inhibitor of enzyme C, causes W and Z to build up.

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