1. Amino acid side chains act as nucleophiles and proton donor/acceptors in various enzymaticreactions. We will use them frequently in reactions during 40B and therefore the purpose of thisexercise is to review the properties of amino acid side chains you have learned in 40A.Ozempic is a medication used for the treatment of type 2 diabetes and an anti-obesity treatment.Ozempic is a modified peptide that mimics the structure of the natural hormone GLP-1.H-His-N GAU-GH₂C CH₂Glu-Gly-Thr-Phe-Thr-Ser Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly Gin-Ala-Ala-a.NHH-His-noH₂C CH₂au PhoPhe-lle Ala Trp Leu-Val-Arg Gly Arg-Gly-OHAdd above the tree-letter code of each amino acid the relevant functional group on its side chain.OHIFor example: -Ser- will be represented by SerNHOHb. The protonation state of each functional group depends on the pH of the solution. Assume thatOzempic is in a solution at pH=7. Draw the functional groups at their correct protonation form.Gu-GyGlu-Gy-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gin-Ala-Ala-Gu Phe-Phe-lle Ala-Trp Leu-Val-Arg-Gly-Arg-Gly-OHOHC. What will be the protonation state of the long non-peptide side chain at pH=7?

Ozempic works like a little coach for your body, helping fight high blood sugar in type 2 diabetes.…

Answered: 1. Amino acid side chains act as…

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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2. Cofactors, coenzymes, and prosthetic groups are important non-protein substances that are required for enzyme function. This is a table of cofactors/coenzymes/prosthetic group we've discussed. Draw the functional portion of the cofactor/pro and explain the functional role in each reaction. a. Cofactor Name thiamine pyrophosphate (TPP) oxidized Lipoamide/lipoic acid/lipoyl-lysine Coenzyme A (CoASH) flavin adenine dinucleotide (FAD) reduced nicotinamide adenine dinucleotide (NADH + H+) oxidized nicotinamide adenine dinucleotide (NADP+) biotin Reaction Pyruvate -> acetaldehyde Pyruvate -> Acetyl CoA aKetoglutarate -> Succinyl-CoA Succinate -> Fumarate Pyruvate -> lactate 6-Phosphogluconate -> Ribulose 5- phosphate Bicarbonate + pyruvate -> oxaloacetate Structure of only the cofactor Functional or catalytic role
4
. The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme C would result in exces- sive urinary excretion of what compound?
A synthetic substrate, the para-nitrophenylacetate (PNPA), is used to monitor enzyme activity of protein P. The product of the hydrolysis reaction absorbs at 410 nm with a molar extinction coefficient of 4 000 M-¹.cm-¹. 1- Write the reaction catalyzed by the protease P using the pNPA substrate. 2- The enzyme extract is too concentrated and a 1/300 dilution is needed for enzyme tests. Considering that you would need at least 600 µL of diluted enzyme extract for activity tests, indicate which volume of buffer and enzyme extract you must use for the dilution.
NH₂ CH3 Methyltransferases NH₂ OH OH S-Adenosylmethionine (SAM) Transamination Phosphate transfer Protein Acetyl transfer Transmethylation CH3 DNÁ CH3 NH₂ What metabolic reaction is best represented by this chemical equation? SAH-Hydrolase (SAHase) NH₂ OH OH S-Adenosyl-L-Homocysteine (SAH) I но. #M OH OH Adenosine NH₂ NH₂ SH Homocysteine
1. Consider the three-dimensional model of the tertiary structure of an enzyme below. Amino acids involved in binding are shaded blue, and amino acids involved in catalysis are shaded red. A. Suppose research has shown that amino acid 82 in the red shaded region is lysine, an amino acid with a positively-charged side chain. This lysine is critical for catalysis. Other studies have found that amino acids 12 and 62 in the blue region are both phenylalanine, an amino acid with a nonpolar side chain, and are critical for substrate binding. These amino acids are relatively close in the active site but are separated by 20-70 amino acids in the primary structure. Using what you know about protein structure, explain how amino acids separated in the primary structure can come close together in the active site. B. Use this information and figure 4.2 in your book to answer the following questions: Do you think changing amino acid 82, lysine, an amino acid with a positively-charged side…
1. Amino acid side chains act as nucleophiles and proton donor/acceptors in various enzymatic reactions. We will use them frequently in reactions during 40B and therefore the purpose of this exercise is to review the properties of amino acid side chains you have learned in 40A. Ozempic is a medication used for the treatment of type 2 diabetes and an anti-obesity treatment. Ozempic is a modified peptide that mimics the structure of the natural hormone GLP-1. a. Gay-The Phe-The-Ser Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gily Gin-Ala-Ala-auhe-s NH C. For example: -Ser- will be represented by Gu Phe-lle Ala-Trp -Leu-Val-Arg-Gly Arg Gly-OH Add above the tree-letter code of each amino acid the relevant functional group on its side chain. OH Ser The protonation state of each functional group depends on the pH of the solution. Assume that Ozempic is in a solution at pH=7. Draw the functional groups at their correct protonation form. O Gu Phe-le- Ala-Trp Leu-Val- Arg-Gly Arg-Gly-OH Quay Thr Phe Thr-Ser…
4.1
From the oligopeptide below, write completely the amino acids and/or peptide fragments that resulted from the reaction of elastase. The amino acids and residues should be represented by the three-letter abbreviation.
15. During vigorous physical activity, a lot of pyruvate is generated inside muscle cells. Show, through a diagram and/or biochemical reactions, two different ways by which this pyruvate is reconverted into glucose. 16. What is the relationship between the amino acid glutamic acid and insomnia (= lack of sleep)?
3. Triose-phosphate isomerase (TPI) catalyzes the movement of a single proton to interconvert dihy- droxyacetone phosphate and glyceraldehyde 3-phosphate in glycolysis and gluconeogenesis. The enzyme, a dimer of identical subunits that are 248 amino acids in humans, has no cofactors, required metal ions, or cooperativity between subunits. The enzyme is found in all tissues. The value of Kcat/KM - 9.2 x 106 sec-'M-1 is close to the rate constant expected for a diffusion-limited reaction. The mechanism of the proton transfer is illustrated in the diagram below. Glu-165 Giu-165 Glu-165 ks HR H 20,PO HO, OH His-95 His-95 His-95 (a) ing structural formulas and naming enzymes and glycolytic intermediates, the reactions of the payoff phase. Consider only anerobic glycolysis. Remember that each glucose molecule yields two mole- cules of glyceraldehyde-3-phosphate (GAP). Indicate the net yield of ATP and NADH generated through anaerobic glycolysis per glucose molecule. The reaction catalyzed by…
If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work? Do not just say yes or no. Give a short explanation for this hypothetical situation.

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