6. Amino acid alanine containing N5 isotope in a-amino group was administratedto mouse with food. It was found that the N5 has rapidly appeared in a-aminogroups of aspartate, glutamate and other amino acids in the liver (with theexception of lysine and threonine). Explain, why does it occur? For the answer:412Chapter 8. Nitrogen metabolisma) draw the reactions of aspartate and glutamate formation with alanineparticipation;b) describe enzymes catalyzing these types of reactions; specify coenzyme;c) specify the group of amino acids due to the possibility that they have beensynthesized in the body and Glu, Ala, and Asp relate to.

The use of radioactive labelling of particular atoms have often been used to determine metabolic…

Answered: 6. Amino acid alanine containing NE…

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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One of the reasons for oxidizing the disulfide bonds in RNase A before removing the urea in the Anfinsen experiment was to demonstrate that ... Urea promotes disulfide bond exchange O Incorrectly-folded proteins lose their enzymatic activity. Urea prevents disulfide bond formation. Urea forms thio-esters with reduced cysteines at pH 8.2 Disulfide bonds are required for enzyme activity.
6
38. The shown reaction is one of the four repeating steps during fatty acid biosynthesis. Which of the following statements is correct? A B CH₂-2-CH₂-2-5-ACP A. The small molecule in box A is NADPH + H* B. It is the second reduction reaction during fatty acid biosynthesis C. Both A and B D. Neither A nor B Он CH3-C-CH₂-C-5-ACP
A 100 mL solution of 0.1 M amino acid (AA) at pH 1.0 was titrated with 1.0 M NaOH solution. The pH was monitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated I to VII. 12 12 II 1097 VI 8. V pH 6 4 39. 120 2 IV 0.5 1.5 2.5 Equivalents of OH
3. (a) Wakil's pioneering studies on fatty acid synthesis included the crucial observation that bicarbonate is required for the synthesis of palmitoyl-CoA. He was surprised to find that very low levels of bicarbonate could sustain palmitate synthesis; that is, there was no correlation between the amount of bicarbonate required and the amount of palmitate produced. Later he also observed that 14C-labeled bicarbonate is not incorporated into palmitate. Explain these observation (b) The condensation reaction catalyzed by B-ketoacyl-ACP synthase generates a 4-carbon unit by combining a 2-carbon unit with a 3-carbon unit and loss of CO2. Write with structural formulas how this occurs. What is the thermodynamic advantage of this way of generating the 4-carbon unit over combining two 2-carbon units as occurs fatty acid oxidation or ketone body reactions" (c) Decide where labeled carbon atoms will be found in palmitate if (i) (3-1“C)malonyl-SCOA or (ii) (2- 14C)malonyl-SCOA are used.
2. (Part A) Coenzyme-dependent enzymes can catalyze the general transformations shown below. What would be the best coenzymes to use for the two steps in the scheme, and why? R CO₂H A R SCOA B R R
11. This below notation represents a Bi-Bi reaction. Aspartate Oxaloacetate a-Ketoglutarate Glutamate Enzyme Enzyme E (E-NH3) (oxaloacetate) (E-NH3) (E-NH3) (a-ketoglutarate) E (aspartate) (glutamate) In this rection, in which step the ternary complex is formed? Briefly explain your answer.
3. (a) In Bakers yeast there are two variants of cytochrome c, a heme containing protein of 108 amino acid residues that catalyzes electron transfer reactions in mitochondria. The two forms of cyto- chrome c known as iso-1 and iso-2 cytochrome c differ in 17 of the 108 amino acids. The content of proton dissociable side chains for the two cytochromes c is given in the table below: Side chain pka iso-1 cytochrome c Ziso-1 iso-2 cytochrome c 12.5 3 4.0 4 8.0 4.0 6.0 10.0 9.0 7.0 4.0 Arginine Aspartate Cysteine Glutamate Histidine Lysine Tyrosine -NH3Ⓡ -COOH 1 4 4 16 5 1 1 What is the overall electrostatic charge on each cytochrome at pH 8? (b) To the right is a diagram of the chemical groups in carboxymethyl-cellulose and DEAE-cellulose that are used for ion exchange chromatography to purify proteins. At pH 8 which chromatographic resin has to be used to separate iso-1-cytochrome c from iso-2-cytochrome c from a lysate of yeast cells? If the proteins are separated by application of a…
A1
1. Draw the products that would be produced from phospholipase C cleavage of a glycerophospholipid with a phosphoserine head group, an alpha linoleic acid attached to C2 of the glycerol and a linoleic acid attached to the C3 of glycerol. Draw these products at pH=1. Be sure to number the fatty acid carbons in your products
о 6. What is the catalytic triad and what particular protein family would you find this? What is the general role of the catalytic triad? Predict what would happen if Asp were mutated to Gly. ructure formation of alpha heli
(Part B) Coenzyme-dependent enzymes can catalyze the general transformations shown below. What would be the best coenzymes to use for the two steps in the scheme, and why? Then, propose an enzyme-catalyzed method for step A to proceed without a coenzyme. Show this enzyme- catalyzed mechanism for step A that does not require the coenzyme. You can abbreviate acidic amino acid residues "Enz-B-H" and basic residues "B-Enz". OH 'R' A R OH 'R' H₂O 'R' B 'R'

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