10. Chymotrypsin is a serine protease enzyme. The Km for the reaction of chymotrypsin withN-acetylvaline ethyl ester is 8.8*102, and the Km for the reaction of chymotrypsin with N-acetyltyrosine ethyl ester is 6.6*10“ M.catalytictriadSer 195His 57Gly 193N-HOHR-N- CaN-HO-C- Asp 102N-acetyl valineN-acetyl tyrosineChymotrypsin Active Sitea. What is the nucleophile here and how is it activated?b. Which substrate has an apparent higher affinity for the enzyme.c. Propose a reason for the difference in affinity based on the shape of each of thesubstrates (see active site figure, cleaves on the C-side of aromatic residues).

a. Serine present in the active site is a nucleophile here and it gets activated by proton…

Answered: 10. Chymotrypsin is a serine protease…

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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1/Vo 1/[S] with I without I with I with I 1/vo without I *-*- 1/vo without I 1/[S] 1/[S] 3. The above graphs are lineweaver-burk plots that demonstrate how inhibitors affect Michaelis Menten enzymes. For each graph identify the type of inhibition and explain how you determined that this enzyme is kinetically demonstrating this type of inhibition.
3. Subtilisin (Mol. weight 27,600) is a protease that can catalyze hydrolysis of certain amino acid esters and amides. For the synthetic substrate N-acetyl-L-tyrosine ethyl ester (Ac-Try-OEt), subtilisn exhibits Km and kcat values of 0.15 M and 550 s-¹, respectively. a) What is the Vmax when the subtilisin concentration is 0.4 mg/ml? b) Indole is a competitive inhibitor of subtilisin with a Ki of 0.05 M. What is the Vmax for Ac-Try-OEt hydrolysis by 0.4 mg/ml subtilisin in the presence of 6.25 mM indole? c) What is the Vo when 0.4 mg/ml subtilisin is incubated with 0.25 M Ac-Try-OEt and 1.0 M indole?
Bovine chymotrypsin is a serine protease. The enzyme is structurally stable over the pH range of 4.0 – 10.0. It exhibits optimum protease activity in the pH range of 7.5 – 9.0, but its protease activity is strongly inhibited at pH < 6.0. Based on your knowledge of serine protease mechanisms, how would you explain this effect of pH on chymotrypsin’s mechanism of catalysis?
Use the two Fischer projections shown below to draw the Haworth projection of these two sugars linked by an a(1-2) linkage, with the ß isoform of the ketohexose. H H ㅎ HO H H OH OH ОН Н НО CH₂OH 애,애애 OH CH₂OH OH H OH OH OH I OH CH₂OH OH OH OH Eng са CH2OH CH2OH OH OH ОН ОН CH₂OH Н OH Н Н OH Н T I CH₂OH CH₂OH OH OH OH CH₂OH CH₂OH Н CH₂OH CH₂OH ОН OH OH НО OH H Н OH CH₂OH
The enzyme lysozyme hydrolyzes glycosidic bonds in peptidoglycan, an oligosaccharide found in bacterial cell walls. The active site of lysozyme contains two amino acid residues essential for catalysis: E35 and D52. Which of the following statements about lysozyme is true? More than one may apply The graph shows the pH-activity profile of lysozyme. 100 50 4. 6. 8. 10 pH Residue E35 exhibits general base catalysis O The pKa of E35 is approximately 4.3 O The pKa of D52 is approximately 4.5 O The optimal activity of lysozyme is approximately 5.2 Residue E35 exhibits covalent catalysis The pka of E35 is approximately 6.1 The pka of D52 is approximately 3.7 Activity (% of maximal)
A certain plant storage protein, after being isolated, was digested using both 8N H2SO4 and conc. Ba(OH)2. The resulting hydrolysates were then analyzed for amino acid composition using paper chromatography with EtOH-NH3-H2O (80:10:10) as the solvent system and ninhydrin as the visualizing agent. Name the amino acids found in the acid hydrolysate labelled 1-5.
The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). [S], M V w/o inhibitor, M/s V w/ inhibitor, M/s 1x10-4 0.0259 0.0098 5x10-4 0.0917 0.040 1.5x10-3 0.136 0.086 2.5x10-3 0.150 0.120 5x10-3 0.165 0.142 In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.
Consider the positively charged amino acid lysine Lys2+ 21 COOH I H&N-C-H I pH 14 12 10 8 6 4 2 0 CH₂ I CH₂ I CH₂ I CH₂ T NH₂+ 0 Nelson p85 2.18 = 2.18 PK₁ Lys+ COO™ I H₂N-C-H H₂N-C-H ī I -----) 8.95 Lysº 8.95 pK₂ pka carboxyl = 2.19 pkaamino = 9.67 pka sidechain = 4.25 COO™ I CH₂ I CH₂ I CH₂ I CH₂ I NH₂¹ 1.0 2.0 Equivalents of OH added- COO™ I H₂N-C-H I 10.79 1 10.79 pk Isoelectric point Lys CH₂2 I CH₂ I CH₂ I CH₂ T NH₂ 3.0 +H3N NH3+ T CH₂ T CH₂ CH₂ CH₂ -COO™ H Lysine (Lys, K) Physiological pH = 7.4 < pl → Amino acid is positively charged at physiological pH 1. Consider glutamate in its fully protonated form (e.g. in a pH = 1 solution) 1) Draw all the forms of glutamate at various pH 2) Calculate the pl of this amino acid 3) Sketch a titration curve showing pH as a function of added [OH-] and locate the predominant forms of histidine in the curve STEPS: 1. Find the H atoms that can be removed on the molecule 2. Associated a pka value to each removable H. 3. Draw the Aa structure at:…
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 schematic representation of the enzyme IspD complexed to inhibitor 3, and a series of inhibitors 3-5 are shown below. Ala202 lle240 mwww NH NH Val263 ОН www HN N- lle177 HN 'N' CI 3 X = N 4 X = C-CN 5 X = C-COO IC50 274 µM IC50 140 nM IC50 35 nM NH2 HN Val266 N -N O-H---- N HN %3D Arg157 HN wwww lle265 Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.
Which of the structures below is that of о-в-D-glucopyranosyl-(1->4)- a-D-glucoругanose CH2OH CH2OH H. OH он H Он OH OH CH2OH HOH2Ć OH он CH2OH CH2OH OH H он H он он CH2OH CH2 OH H OH он OH None of the other structures are correct.
A biochemist is trying to determine the type of proteases they have isolated from walrus blubber. The three proteases and their relative activities in the presence of the indicated non-specific irreversible inhibitors are shown in the table below: Protease a Protease B Protease y Given this data, please answer the following question: The catalytic site of Protease y contains an important: с H Y + lodoacetate Normal Activity Normal Activity No Activity R + Tetranitromethane Normal Activity No Activity Normal Activity

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