Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (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 190 Val 216 Asp 189 Chymotrypsin Trypsin Elastase
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- Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (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 190 Asp 189 Chymotrypsin Trypsin ElastaseWhat are the amino acids of the catalytic triad of chymotrypsin? State the mode of catalysis shown by each of the amino acids that you have named. (a) (b) Predict what will happen if aspartic acid of the triad is replaced by asparagine. (c) Briefly explain the role of the oxyanion hole for the catalysis of chymotrypsin.(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?
- Which folate structure (from the list below)(a) is the substrate for the enzyme that is inhibited by methotrexate andtrimethoprim?(b) has the most highly oxidized one-carbon substituent?(c) is used in the conversion of serine to glycine?(d) transfers its one-carbon substituent to a B12 coenzyme? What amino acid is synthesized as the end result of this reaction?(e) is the coenzyme for the thymidylate synthase reaction?(f) is not known to exist in nature?(g) is used in purine nucleotide synthesis?How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?the structures of chymotrypsin and other serine proteases revealed that the active sites of these enzymes shared a particular sterochemical arrangement of residues crucial to their activity. This came to be known as the catalytic triad, as it consisted of the oponyomous serine (Ser) residue, along with a histidine (His) and an aspartate (Asp) residue. Which of the following would result in the greatest decrease in function of the catalytic triad found in serine proteases? O Mutation to Ser, Cys, Asp O Mutation to Ser, His, Asp O Mutation to Cys, His, Asp O Mutation to Ser, His, Glu
- You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new enzyme uses the same catalytic triad and the same reaction mechanism as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non-ionizable R groups. a) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn-Phe-Lys substrate ending your answer with product and free enzyme. b) From the list below, which of the components would most likely be found in the area of the enzyme that substitutes the hydrophobic pocket of chymotrypsin? Very briefly explain your choice(s)., Ser lle Zn Val c) You've constructed a molecule that is able to bind to the 1 tetrahedral intermediate of your new.enzyme, preventing catalysis. From experimental results, you can see that this molecule is only able to bind to the tetrahedral intermediate. Assuming that this enzyme follows…You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new enzyme uses the same catalytic triad and the same reaction mechanism as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non- ionizable R groups.A) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn- Phe- Lys substrate ending your answer with the product and free enzyme.You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new enzyme uses the same catalytic triad and the same reaction mechanism as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non- ionizable R groups. A) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn- Phe- Lys substrate ending your answer with the product and free enzyme. B) From the list below, which of the components would most likely be found in the area of the enzyme that substitutes the hydrophobic pocket of chymotrypsin? Very briefly explain your choice(s): Ser ile Zn+ Val C) You've constructed a molecule that is able to bind to the 1st tetrahedral intermediate of your new enzyme, preventing catalysis. From experimental results, you can see that this molecule is only able to bind to the tetrahedral intermediate. Assuming that this enzyme follows…
- Many phospholipase C enzymes contain pleckstrin homology (PH) domains. What is the function of these domains? (a) Bind DNA, (b) Phosphorylate proteins, (c) Phosphatase proteins, (d) Bind proteins, (e) Bind phosphatidylinositol. I note that PH domain interacts with 3’phosphoinositides, contributing to recruitment of AKT to the plasma membrane, thus thinking of the possible answer (e) which is phosphatidylinositol (ie. PI) of a family of lipids consisting PIP3 or PIP2 etc. However, I wonder if “3’phosphoinositides” is the same as “PIP3”.As an alternative, I note that PH domain is a protein domain that occurs in a wide range of proteins involved in intracellular signaling, I tend to choose (d) as an answer also.I should be grateful for receiving your expert advice as to which (a) to (e) is the best answer.(b) Biotin is a coenzyme required for a key step in gluconeogenesis. (i) To which enzyme is biotin linked and what is the nature of the bond? (ii) What properties do the biotin and the linkage have that enable biotin to interact with two distinct active sites in this enzyme? (iii) What chemical steps take place at each of these active sites (no need to specify the complete reactions)?Serine Proteases, such as chymotrypsin, contain Ser/Asp/His as a catalytic triad (i.e. three collaborating amino acids) of amino acids involved in enzyme catalysis. Why is this? Examine each amino acid of this catalytic triad (schematically detailed below: Ser195/Asp102/His57) and, based on your understanding of amino acid characteristics, predict what the role of each amino acid could be. His57 Ser195 Asp102