Chymotrypsin, trypsin, and elastase are digestive enzymes called scrine proteases. The serine proteases differ in substratespecificity. Chymotrypsin cleaves peptide bonds after aromatic or bulky hydrophobic side chains, trypsin requires basic aminoacid residues, and elastase cleaves bonds following small uncharged side chains. Refer to the chart of amino acids.The specificity pockets (substrate-binding sites) of each of the serine proteases are shown in the images. The substrate aminoacid side chains are shown in each pocket.Determine which specificity pocket is a part of each enzyme. Match each specificity pocket to the appropriate enzyme.ChymotrypsinTrypsinAssuer BakWhich of the following amino acids haye side chains that fit into the specificity pocket of trypsin. Select more than onelysineaspartatearginineglycinephenylalaninem RNase is an enzyme that cleaves the PO bond in RNA. It has two His residues in the active site. Suggest a plausibleexplanation why the enzyme activity changes when pH is increased or decreased from pH 6.0, as shown in the graph.Choose all of the true statements.80There are two His residues and both are deprotonatedbelow pH 4.2.0020The substrate is affected by the change in pH and isinactive (postively charged) when pH is above 6.0.The RNase reaction is an example of metal ioncatalysis with a positively charged metal.OHBoth His residues are deprotonated at pH higher thanthan 6.5.Data provided by Dr. Sunita Chowrita, University of British ColumbiaOne His residue abstracts a proton from the substrateat pH 6.0, whereas the other donates a proton.

Aminoacids are classified based on the nature of their side chain. They are Acidic aminoacids :…

Answered: Chymotrypsin, trypsin, and elastase are…

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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Determine whether each of the examples or phrases describes an essential amino acid, a nonessential amino acid, or both essential and nonessential amino acids. A table of amino acids. Essential amino acids branched-chain amino acids derived from 3-phosphoglycerate, a glycolytic intermediate methionine threonine Nonessential amino acids Answer Bank an amino acid synthesized from pyruvate in humans synthesized by humans obtained from food only Both the amino acid that is a thioether
Estimate the concentration of an enzyme in a living cell. Assume that fresh tissue is 80% water and all of it is intracellular, the total soluble protein in a cell represents 15% of the weight, all the soluble proteins are enzymes, the average weight of a protein is 150000 and about 1000 different enzymes are present.
The amino acid residue sequence of the hemoglobin beta subunit polypeptide would represent what type of structure? O PRIMARY O SECONDARY O TERTIARY O QUATERNARY
Which of the following amino acids would most likely exhibit hydrophobic interaction with isoleucine? Oserine Omethionine Oglutamate threonine arginine Previous M
Assuming the oligopeptide ALPHAHELICKS forms one continuous α helix, the carbonyl oxygen of the glutamic acid residue is hydrogen bonded to the amide nitrogen of? Isoleucine Cysteine
From the oligopeptide below, write completely the amino acids and/or peptide fragments that resulted from the reaction of pepsin. The amino acids and residues should be represented by the three-letter abbreviation.
Drugs are small molecules that often occur in either a neutral or a charged form, depending on pH. For example, aspirin can be either neutral or lose a proton to be negatively charged. When aspirin is charged, it does not diffuse well into the body. pH varies in the gastrointestinal track. Since the stomach has a low pH (pH=3), it has a larger concentration of neutral aspirin (10-3 M), while the small intestine (pH=6) has a smaller neutral aspirin concentration (10-6 M). For the following, assume that the neutrally charged aspirin molecule has a diffusion coefficient through the cell of 1 x 10-6 cm2/s. C) We’d like to figure out where in the body aspirin is absorbed as determined by its diffusion rate. If the small intestine has a surface area 50 times that of the stomach, what is the ratio of the diffusion rates in the stomach compared to the small intestine? D) In which part of the GI tract is most of the aspirin absorbed?
Which of the following mutations is most likely to cause the aggregation of a protein? the mutation of a surface glu to an asp the mutation of an interior val to an ile the mutation of a surface glu to a val the mutation of a surface thr to a glu the mutation of an interior thr to a ser
What will at the position of "Question mark" . Identify and explain?
Describe with detail the chemical reactions of 5 proteins that are involved in human metabolic disorders. Explain in detail the interaction mechanisms with their corresponding substrates, their reaction mechanisms, and chemical regulations.
The biological marcomolecules composed or multiple units of amino acids is
Given the following decapeptide sequence, which aminoacids would you expect to be on the surface of this moleculeonce it folds into its native conformation?Gly—Phe—Tyr—Asn—Tyr—Met—Ser—His—Val—Leu

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