6. The reagent dithiothreitol (DTT) is commonly used to reduce disulfide bonds inProteins. The mechanism of this reduction reaction is analogous to that for thebeta-mercaptoethanol reduction of disulfide bonds, except that only a singlemolecule of DTT is involved in the mechanism and a cyclic disulfide oxidationproduct is formed. Draw a diagram of the mechanism of the DTT-mediateddisulfide bond reduction reaction.H-S-CH₂-CH-CH-CH₂-S-HTIHO OHDTT

DTT works as a reducing agent by donating electrons to break disulfide bonds in proteins, leading to…

Answered: The reagent dithiothreitol (DTT) is…

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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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
7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent
(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?
16. The overall reaction for the glycolysis reaction is C6H₁2O6(aq) + 2NAD+ (aq) + 2ADP³(aq) + 2HPO(aq) + 2H₂O(1) 2CH3COCO₂ (aq) + 2NADH(aq) + 2ATP4 (aq) + 2H3O+ (aq). What is A,G at chemical equilibrium?
1 ).Which of the following accurately describes substrate specificity for serine proteases? A.The binding cleft B.Mg2+ metal activated enzyme C.The catalytic triad D.Facilitates redox chemistry E.Stabilizes the transition state 2). Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? select all that apply leucine aspartic acid histidine lysine Please answer both correct i will give u upvote.
17. Omeprazole is a bioprecursor prodrug that is activated by protonation to give active metabolite that inhibits H¨,K*-ATPase covalently. By using chemical equations show activation of Omeprazole and its reaction to inhibit the H*,K*-ATPase. CH3 H3CO. s=0 H3C HNN Omeprazole OCH3 18. The following compound is an open-chain prodrug of benzodiazepines which undergo N- dealkylation to triazolam. Using chemical equations show transformation of this prodrug to triazolam. H3C H3C CH3 CH3 triazolam open-chain prodrug of triazolam
5) A certain aerobic organism is able to metabolize the following glycolipid: "CH,OH OH HO OH A. Draw the 2 resulting structures that would occur upon initial hydrolysis of the O-glycosidic bond. B. Calculate how much ATP is formed upon complete aerobic oxidation of one mole of the compound. Assume that no ATP is produced when one mole of the glycosidic bond in the above compound is hydrolyzed. Show calculation below.
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…
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…
15. Write the metabolites of the following substrates due to phase Il reactions: a. b, R R C. R R NH ΝΗ LOH 3'-phosphoadenosine-5'-phosphosulfate Enzyme S-adenosylmethionine Enzyme Acetyl-SCOA
2. ( the active site in the Michaelis complex of a-chy- motrypsin and a polypeptide substrate. Describe briefly the catalytic or structural roles of the : To the right is a schematic diagram of His $7 residues listed below: HOSer 195 (а) Ser195 AAn-C-ÇH-NH-Ç ÇH-NH -AAn R H H. -N- 195 193 Gly Ser (b) His57 (c) NH groups of Gly193 and Ser195 (d) The most favorable side chain R for binding (e) Identify the scissile bond with an arrow, i.e., the bond in the peptide substrate that is cleaved as a result of the catalytic action of the enzyme. You can point to it on the diagram above.
15. Write the metabolites of the following substrates due to phase Il reactions: a. b. R R C. R R NH NH LOH 3'-phosphoadenosine-5'-phosphosulfate Enzyme S-adenosylmethionine Enzyme Acetyl-SCOA

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