The compound below is an affinity label for the enzyme trypsin. H2N. NH2 NH H3C Provide detailed answers the following questions. a) What are the important parts of this molecule that allow it to function as an affinity label? b) Why is this molecule specific for trypsin and not chymotrypsin or elastase? c) How does this compound react with the enzyme and what amino acid(s) are involved? ZI

The compound below is an affinity label for the enzyme trypsin. H2N. NH2 NH H3C Provide detailed answers the following questions. a) What are the important parts of this molecule that allow it to function as an affinity label? b) Why is this molecule specific for trypsin and not chymotrypsin or elastase? c) How does this compound react with the enzyme and what amino acid(s) are involved? ZI

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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There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…
b) Consider the following experimental results: Total hydrolysis of a nonapeptide gave: Ala,Arg, Glu,Leu,Lys,Met,Phe,Tyr,Val One fragment from CNBR treatment was: Tyr-Leu-Lys One fragment from Chymotrypsin treatment was Arg-Glu-Met-Tyr One fragment from Trypsin treatment was Val-Ala-Phe-Arg i. Deduce, with suitable explanations, the amino acid sequence of the nonapeptide.
Ceruloplasmin is a blue-colored monomeric oxidase found in mamma- lian blood plasma. It contains multiple copper atoms per mole- cule. A ribbon representation of its three-dimensional shape is shown below: a) b) c) Identify any cofactor(s) which ceruloplasmin may possess. How do you know? Does ceruloplasmin act as an enzyme ? Describe the secondary, tertiary and quaternary structures of ceruloplasmin.
Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, III
b) Consider the following experimental results: Total hydrolysis of a nonapeptide gave: Ala,Arg,Glu,Leu,Lys,Met,Phe,Tyr, Val One fragment from CNBr treatment was: Tyr-Leu-Lys One fragment from Chymotrypsin treatment was Arg-Glu-Met-Tyr One fragment from Trypsin treatment was Val-Ala-Phe-Arg ii. The reagent shown below is widely utilized in the sequencing of peptides. Treatment of the nonapeptide you deduced in part i. with this reagent yields a phenylthiohydantoin derivative, compound 1, and an octapeptide. Write a mechanism for the formation of compound 1. N=c=8
H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14
Determine the sequence of the decapeptide given the following information below. The decapeptide was hydrolyzed and confirmed to contain these amino acids: E, F, K, M, Q, S, T x 3, W Edman degradation product of the decapeptide: T trypsin fragments: a tetrapeptide (F,K,Q,T) and a hexapeptide (E,M,S,2T,W) chymotrypsin fragments: free S, a dipeptide (F,T) and a heptapeptide (E,K,M,Q,T,T,W) CNBr treatment of the heptapeptide (E,K,M,Q,T,T,W) yielded a tetrapeptide (K,T,M,Q) and a tripeptide (E,T,W) Edman degradation product of (E,T,W): E Use one-letter abbreviations only. One amino acid per blank.
For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s -1 , k-1 = 3.1 ⅹ 104 s -1 , and k2 = 3.4 ⅹ 105 s -1 . a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach rapid equilibrium or the steady state? Show work justify b) What is kcat for this reaction? Show work justify c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1 , and each enzyme has two active sites.
(a) The octapeptide AVGWRVKS was digested with the enzyme trypsin . Which method would be most appropriate for separating the products: ion-exchange or gelfiltration chromatography? Explain. (b) Suppose that the peptide was digested with chymotrypsin . What would be the optimal separation technique? Explain.
An enzyme catalyzes the reaction M ßàN. The enzyme is present at a concentration of 1 nM, and the Vmax is 2 M s-1. The Km for substrate M is 4 μM. a)Calculate kcat. b)What values of Vmax and Km would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an α’ of 2.0?
Consider the enzyme pancreatic amylase, which has an optimum pH of 7.0. How is the rate of a pancreatic amylase-catalyzed reaction affected by each of the following changes: (a) lowering the pH from 7 to 4; (b) increasing the pH from 7 to 9; (c) decreasing the temperature from 37 °C to 28 °C; (d) increasing the temperature from 37 °C to 50 °C?
Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.