Draw each of the enzymatic step for each chemical conversion and write the enzyme togetherwith the co-factor for the steps where a co-factor is involved.How many carbons are transferred in the conversion from step 1 into the intermediate from step2?Step 1OHACP-s? (multiple enzymatic steps)OHOHStep 2ACP-SR15..

Fatty acid biosynthesis is the pathway of synthesizing fatty acids from acetyl-CoA and NADPH…

Answered: Draw each of the enzymatic step for…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 21P: Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved...

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Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
For the following two scenarios, sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction. For each of these, overlay the free energy diagram for the uncatalyzed reaction and indicate AAG" on your sketch: a). Substrate binding is rate limiting b). The chemical step is rate limiting
Please note the reaction expression below. Which of the following rate constants describes the breakdown of the enzyme-substrate complex? There may be more than one answer. k₂ E+S OK-2 U k₂ 0 k₁ OK.1 k3 k.3 SES EPE+P K.3 K.₂ k.
Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate  delta delta G〒 on your sketch: Chemical step is rate limiting
A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates. It is impossible for this result to be true. OA. Adding the substrate increases the weak forces that stabilize the enzyme. OB. The high concentration of substrate forms a barrier around the hexokinase. D. Adding the substrate results in protective covalent bonding.
Because it resembles the two physiological substrates, phosphonacetyl L - aspartate (PALA) is a strong inhibitor of ATCase. Low concentrations of this unreactive bisubstrate analog, on the other hand, enhance reaction velocity in the presence of substrates. The reaction rate rises as PALA is added, until three molecules of PALA are attached per molecule of enzyme. This maximum velocity is 17 times higher than it would be without PALA. With the addition of three additional molecules of PALA per molecule of enzyme, the reaction rate drops to practically nil. Why does PALA activate ATCase at such low concentrations?
a) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and D-DOPA? Show any relevant analyses or calculatins you did to determine these values. ( HINT a graph might be helpful here! ) b) Based on your answer to part a, briefly describe how the kinetics of the enzyme differs for the two substrates. Which Substrate has better binding affinity to the enzyme
k_1 E + SES E + P +0 k₂ S ↓↑ KIS ESS Based on this model, please answer the following questions: i) This is the model for what? Uncompet tive ii) Show the rate equation for an enzyme reaction of this type. iii) Show the Lineweaver-Burk plot for this case. A
During chymotrypsin-mediated catalysis, which of the following statements is true? Select any/all answers that apply. O A. A basic (positively-charged) side chain of the substrate polypeptide sits within the oxyanion hole of the enzyme. O B. A basic (positively-charged) side chain of the substrate polypeptide sits within the specificity pocket of the enzyme. O C. Ser195 hydrogen-bonds with the backbone carbonyl group of the substrate polypeptide within the oxyanion hole of the enzyme. O D. All three residues that comprise the catalytic triad of the enzyme interact directly with the substrate polypeptide chain. O E. Both covalent catalysis and acid-base catalysis occur.
Consider this intermediate in the derivation of the Michaelis-Menten equation. [E] [S] [ES| k-1 + kz km Assume that k is negligible compared to the other rate constants. If the k is very small, it suggests that the enzyme has a Select an option affinity for its substrate, while if the if the km is very large, it suggests that the enzyme has a Select an option. affinity for its substrate. Select an option Submit You have used 0 of high Sav low moderate
You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphatase
Consider two enzymes catalyzing two reactions (A --> B --> C ) in a metabolic cascade with their properties summarized below: Keg (for reaction) Enzyme Reaction KM Kcat / KM 102 M-1s-1 108 M-1s-1 1 A --> B 1 1 mM 2 B --> C 10 10 mM Initial concentrations are [A] = 0.1 mM and [B] = [C] = 0 and both enzymes are present at concentrations of 1 mM. After waiting for 1 ms, the concentrations of A, B, and C are measured. How do you expect the concentrations to be ordered? O [B] > [A] > [C] O [C] > [B] > [A] O [A] > [B] > [C] O [A] > [C] > [B] [C] > [A] > [B]

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Draw each of the enzymatic step for each chemical conversion and write the enzyme together with the co-factor for the steps where a co-factor is involved. How many carbons are transferred in the conversion from step 1 into the intermediate from step 2?