need answer in detail 2.Given the following biosynthesis scheme, answer the questions (a)-(c) below.OHOHMeCEMeMeSACPOHOHAMeMeMeSACPSACPDSACPMeBOHMeMeMeSACPSACP(a) Determine the missing enzyme, or sequence of enzymes, involved in the stepsA-E. The answers must include the name of the enzyme, or its two-letter abbreviation,together with any relevant co-factors involved with the individual enzymes. For the stepsinvolving more than one enzyme, the correct order in which they are used must be clearlyindicated.(b) Draw the structures of the two different enzyme bound substrates involved in steps B andD, respectively. Abbreviations for the attached enzymes are acceptable (eg. ACP).(c) Draw the structures of the TWO biosynthetic intermediates formed during step C.

For the synthesis of unbranched fatty acids, living beings carboxylate Acetyl CoA to yield malonyl…

Answered: Given the following biosynthesis…

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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11. The most highly sensitive test in viral hepatitis is y-Glutamyl transpeptidase (Y-GT) increased activity in blood, which level riscs 10-15 times more than the norm (30-50 ME/L). What is the diagnostic value of this enzyme? For the answer: a) present the main properties of enzymes which activity determination in patient blood are widely uscd in enzyme diagnostics; b) explain the y-Glutamyl transpeptidase (y-GT) system and present an appropriate scheme; c) give examples of other enzymes which activity is determined in the liver disorders.
1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:
3. (a) The activity of the Pentose Phosphate Pathway is commonly quantified by measuring 14CO2 production from C-14 labeled glucose. In this assay, glucose is metabolized aerobically by cells or tissue slices; both [1-14C] glucose and [6-14C] glucose are employed separately but in parallel. This classical method, thus, requires two separate assay mixtures. Which radioactive isotopomer of glu- cose releases 14 CO2 generated by the Pentose Phosphate Pathway? Confirm your conclusion by drawing the intermediates of the oxidative phase of the PPP with structural formulas, starting with glucose-6-phosphate. Name the intermediates and indicate enzymes. (b) ( Because the assay protocol requires aerobic incubation of cells or tis- sue slices with isotopically labeled glucose in parallel assays, what is the purpose of the other radioactive glucose derivative? To answer this question base your answer using the diagram on the right. O2 NADH CH₂OH + 2 NAD+ HO HO + 2 Pj 2 CO + 2 ATP HO OH 2 ADP CH3…
3. (a) The activity of the Pentose Phosphate Pathway is commonly quantified by measuring 14CO2 production from C-14 labeled glucose. In this assay, glucose is metabolized aerobically by cells or tissue slices; both [1-14C] glucose and [6-14C] glucose are employed separately but in parallel. This classical method, thus, requires two separate assay mixtures. Which radioactive isotopomer of glu- cose releases 14 CO2 generated by the Pentose Phosphate Pathway? Confirm your conclusion by drawing the intermediates of the oxidative phase of the PPP with structural formulas, starting with glucose-6-phosphate. Name the intermediates and indicate enzymes. (b) ( Because the assay protocol requires aerobic incubation of cells or tis- sue slices with isotopically labeled glucose in parallel assays, what is the purpose of the other radioactive glucose derivative? To answer this question base your answer using the diagram on the right. O + 2 NADH CH₂OH + 2 NAD+ ○ HO HO + 2 Pi 2 CO + 2 ATP HO OH 2 ADP…
There are six classes of enzymes, namely oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. (i) (ii) Cell disruption is one of the steps performed during enzyme production. Explain the reason of performing cell disruption in enzyme production and provide THREE (3) enzyme extraction methods for this type of enzyme. Explain the principles of gel electrophoresis as one of the methods used for enzyme purification.
5. Shown below are the first steps in the mechanism of a cysteine protease, which catalyses amide bond hydrolysis in a similar manner as serine proteases. (a) Complete this mechanisms, and (b) sketch the approximate reaction coordinate diagram for this catalyzed reaction relative to the uncatalyzed proteolysis. HN N HN cysteine protease
3. (a) The beakers below represent different conditions for measuring the initial velocity (vo) of an enzyme-catalyzed reaction under the steady-state approximation. The gray "donut-shaped" struc- tures represent the enzyme. The blue, filled circles represent free substrate molecules. The red cir- cles represent substrate molecules bound in the active site of the enzyme forming the Michaelis (ES) complex. Indicate in the diagram of the double reciprocal plot which kinetic parameters or variables each of the three "beaker conditions" represent either alone or in combination with another. A B 455 C V₁™¹ [So]-¹
7. To what main enzyme class do the enzymes that catalyze the following reaction belong? (Oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) со о 8. Label the following as examples of a "lock and key" model or an "induced fit" enzyme model? substrate a. b. tive sihe a. b. yme-bstrate comples
6) What is the approximate temperature (in both F° and C°) for enzyme activity in the human body?
The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is A
A TAMU undergraduate biochemistry student is tasked with characterizing a new enzyme. After devising an assay, the student does some initial experiments. When initiating the reaction by adding the enzyme to a solution of substrates (but no products) she finds that at the earliest times the change in the [A] is non-linear and increasing and then becomes linear for awhile and then decreases eventually to zero. Explain what is unusual and what various aspects of the time course mostly likely means.
5. Gout can be caused by superactivation of PRPP synthase, or partial deficiency of hypoxanthine-guanine phosphoribosyl transferase. Why the change in these enzyme activities can induce the development of this disorder? For the answer: a) write down the scheme of the reactions catalyzed by these enzymes;b) specify metabolic pathways these reactions take part in; c) answer the main question of the problem.

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