Q20: Which amino acids have side chains that fit into the specificity pocket of elastase?glycineaspartatealaninelysinetyrosinearginine Chymotrypsin, trypsin, and elastase are digestive enzymes called serine 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. A chart of amino acids is available foryour reference.Determine which specificity pocket is a part of each enzyme.ChymotrypsinTrypsinAnswer BankWhich amino acids have side chains that fit into the specificity pocket of elastase?Elastase

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

Answered: Chymotrypsin, trypsin, and elastase are…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 14QP: If phenylalanine was not an essential amino acid, would diet therapy (the elimination of...

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The substitution of a Glutamate residue for Valine residue is a conservative substitution. TrueFalse
a protease that cleave peptide bonds adjacent to aspartate and glutamate would likely have an s1 pocket that contain positively charged amino acids true or false
Describe the structures of glutamine and alanine. What are the characteristics of the R-groups? What other features of these amino acids make them important as they relate to metabolism?
pyrenylmaleimide could react with which amino acids? Why the lifetime of a prtein will reduce once conjugated pyrenylmaleimide.
Given the peptide Val-Ser-Gln-Lys The lateral chain of one of these amino acids can be modified by N-acetylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7 The lateral chain of one of these amino acids can be modified by phosphorylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7.
Draw the structure of the α-keto acid formed by the transamination of each amino acid: (a) tyrosine; (b) asparagine.
In some proteins, the side chain of serine appears to undergo ionization. Explain why ionization would be facilitated by the presence of an aspartate residue nearby.
Illustrate the pathways to synthesize the following aminoacids:a. glutamineb. serinec. arginined. glycinee. cysteine
From the peptide chain: Met-Tyr-Phe-Arg-Ile-Glu-Asn-Asp-Ser, draw the structure of the product formed when reacted with Elastase
If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work? Do not just say yes or no. Give a short explanation for this hypothetical situation.
What type of noncovalent interaction occurs between the glutamine and threonine side chains? Draw the structures of these amino acids to show the interaction.
Peptide YY (PYY) is a 36-amino acid peptide that is so named because it contains twobiochemically relevant tyrosine residues.Describe the function of PYY and state where it is synthesized.

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