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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Similar questions

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
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
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
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.
List the name of two amino acids that belong to each of these type of amino acids: Nonpolar (hydrophobic) polar(uncharged) positively charged (basic) negatively charged (acidic)
Which of the amino acids will nearly always be found buried in the center of proteins? valineglycinelysineglutamic acid
describe the biochemical function and mode of action of branch chain amino acids in biochemistry terms
Amino acids with ionizable side chains are found in all groups except: negatively-charged positively-charged polar hydrophobic
Reductase is the Fe protein composed of two: polypeptide chains linked by three disulfide bonds. polypeptide chains linked by a 4Fe–4S cluster. α subunits and two β subunits. polypeptide chains linked by a 2Fe–2S cluster.
Researchers have identified an enzyme that can catalyze two different chemical reactions. Which of the following is most likely true based on this finding? A B C D The reactants involved in the two reactions are very similar in their charge and shape. The reactant in one reaction acts as an allosteric inhibitor while the reactant in the sec- ond acts as an allosteric activator. The enzyme contains both alpha-helices and beta-sheets in their secondary structures. The catalytic activity of the enzyme is dependent on both competitive inhibition and al- losteric regulation.
Can you explain why this is ?

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