Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have differentspecificities.(a) These proteases are considered serine proteases because the active sites contain serine, histidineand aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing proteinsubstrates.(b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below.Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala,Arg, or Trp? Explain your answers.Val 216KVal 190Asp 189ChymotrypsinTrypsinElastase

Proteases are enzymes that cleave polypeptide chains. They all hydrolyze the peptide bond present in…

Answered: Chymotrypsin, trypsin, and elastase all…

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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the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.
Describe the features of the first binding site (for allosteric enzyme unprotkb-p39086), including structural features that recognize and complement the first ligand.
The graph displays the activities of wild-type and several mutated forms of subtilisin on a logarithmic scale. 5 The mutations are identified as: • The first letter is the one-letter abbreviation for the amino acid being altered. • The number identifies the position of the residue in the primary structure. The second letter is the one-letter abbreviation for the amino acid replacing the original one. • Uncat. refers to the estimated rate for the uncatalyzed reaction. Log ₁0k cat (S-¹) -5 -10 Wild type D32A S221A H64A İnti. S221A H64A D32A Uncat. How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in the catalytic triad mutated compare to the activity of the uncatalyzed reaction? O It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster…
Trypsin contains a/an [aspartate/serine/histidine] in its specificity pocket to attract lysine and arginine side chains. It contains a potent nucleophilic [histidine/serine/aspartate] in its active site that is capable of attacking the electrophilic [carbon/nitrogen/oxygen] of the closest peptide bond. The [acyl-enzyme/specificity pocket/oxyanion] transition state is stabilized by the backbone amide hydrogens of glycine and serine. In this way, the enzyme is able to catalyze the [hydrolysis/ligation/metalysis/hydrogenation] of the peptide bond.
You are studying the kinetics of a novel competitive inhibitor of ATP-citrate lyase that can be used to prevent obesity. What is likely true about this inhibitor? (A) This inhibitor lowers the Vmax of ATP-citrate lyase. (B) The inhibitor likely looks structurally similar to acetyl CoA. (C) The inhibitor binds to an allosteric region on ATP-citrate lyase and prevents catalysis. (D) You can distinguish between an uninhibited and inhibited enzyme by comparing the x-intercepts on a Lineweaver-Burk plot. (E) This inhibitor lowers the KM of ATP-citrate lyase. Related to this question, you should also be able to: • explain the function of ATP-citrate lyase and why inhibition would prevent obesity • interpret Michaelis-Menten & Lineweaver-Burk plots related to this question • explain the differences between a competitive and non-competitive inhibitor
In the: Presence of competitive inhibitors of peptidyl transferase. Explain: (a) What is the process affected? (b) What is the Effect on the process? (c) Does it affect prokaryotes, eukaryotes or both?
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, proposean enzyme-catalyzed method for step A to proceed without a coenzyme. Show this enzymecatalyzed mechanism for step A that does not require the coenzyme. You can abbreviate acidicamino acid residues “Enz–B–H” and basic residues “ B–Enz”.
serine proteases act via a two-step catalytic mechanism. However, as a critical scientist, you may want to see data that supports this claim. One experiment that can provide such evidence is called a 'pre-steady state' kinetics experiment using the chromogenic substrate, N-acetyl- phenylalanine p-nitrophenyl ester. As shown below when this substrate is cleaved, the p-nitrophenylate is a yellow product whose absorbance can be measured in real time using a spectrophotometer. When the chromogenic substrate is rapidly mixed together with a limiting amount of protease enzyme, the accumulation of product is measured right away on fast (millisecond) timescales. In this experiment, one observes two distinct phases of the reaction as shown in the plot below. Based upon what you know about the mechanism of serine proteases, provide a mechanistic interpretation for the observation of these two phases of the reaction. + H₂O N-Acetyl-L-phenylalanine p-nitrophenyl ester p-Nitrophenolate Absorbance…
From the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?
“Caspase” describes the catalytic activity of this enzyme. What amino acyl residue participates in the catalytic mechanism? What substrate motif does caspase-8 recognize?
The effect of ATP on the allosteric enzyme PFK-1 is shown below. For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but a point is reached beyond which increasing the concentration of ATP inhibits the enzyme. (a) Explain how ATP can be both a substrate and an inhibitor of PFK-1. How is the enzyme regulated by ATP? (b) In what ways is glycolysis regulated by ATP levels? (c) The inhibition of PFK-1 by ATP is diminished when the ADP concentration is high, as shown in the illustration. How can this observation be explained? *A graph is included for this question*
Determine the amino acid sequence of Peptide A, which was obtained by hydrolyzing a larger peptide with trypsin, using the data below: Total hydrolysis of Peptide A produces (Ala2, Arg, Glu, Gly, Met, Pro2, Ser, Tyr). Sequential Edman degradation of Peptide A produces a derivative of Ala in the first cycle; a derivative of Serine in the second cycle; and a derivative of Proline in the third cycle. Cleavage of Peptide A with chymotrypsin yields two peptides: a tripeptide III containing Ala, Arg and Gly; and a heptapeptide IV containing Ala, Glu, Met, Pro2, Ser and Tyr. Edman treatment of tripeptide III generated a derivative of Alanine. Cleavage of Peptide A with cyanogen bromide (which cleaves peptides on the C-terminal side of Methionine) yields two pentapeptides labeled I and II. Total hydrolysis or peptide I indicate that it contains Ala, Arg, Gly, Pro and Tyr; pentapeptide II contains Ala, Glu, Met, Pro, and Ser.

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