7.
Based on the knowledge of the catalytic triad, chymotrypsin will not be functional at a pH of 7.
Based on what you know of the catalytic triad, at which pH will Chymotrypsin not be...
The chymotrypsin catalytic triad contains one Histidine and one Serine residue. Explain, in some detail and in chemical terms, how an a) a Histidine to Alanine mutation, and b) a Serine to Cysteine mutation in the chymotrypsin catalytic triad might affect catalytic activity of this enzyme.
The structure of the active site of chymotrypsin is shown below. The catalytic triad shown (Ser 195, His 57, and aspl02) are shown. A peptide with a phenylalanine is shown bound in the active site. 1. Chymotrypsin is a serine protease. The Km for chymotrypsin with N-acetylvaline ethyl ester is 8.8 X 102 M. The Km for the reaction with N-acetyltyrosine ethyl ester is 6.6 X 10 (a) Which substrate has the higher affinity for this enzyme? (b) Give a...
What is the catalytic triad of chymotrypsin, a type of serine protease? the enzyme-cofactor-intermediate complex the amino acids serine, histidine, and aspartate the amino acids cysteine, histidine, and aspartate the enzyme-cofactor-substrate complex the amino acids serine, histidine, and glutamate
Based on what we've learned about the enzyme chymotrypsin: a) Explain the general role of each catalytic residue in the chymotrypsin catalytic triad. b) Describe the catalytic strategy or strategies used by chymotrypsin. c) Identify the class of enzymes chymotrypsin belongs to. 7. At a molecular level, how do carbon dioxide and hydrogen ions regulate oxygen binding to hemoglobin?
The catalytic efficiency of many enzymes depends on pH. Chymotrypsin shows a maximum value of k_cat/K_M at pH 8. Detailed analysis shows that &k_cat increases rapidly between pH 6 and 7 and remains constant at higher pH. K_M increases rapidly between pH 8 and 10. Suggest explanations for these observations. Match the words in the left column to the appropriate blanks in the sentences on the right. Make certain each sentence is complete before submitting your answer.
Please carry out a table-based comparison between the catalytic mechanisms of chymotrypsin and lysozyme. THANK YOU
What do the catalytic mechanism of the enzyme lipase and the catalytic mechanism of chymotrypsin have in common, what is different? What is the reason for the observed differences? Compare them step by step.
Trypsin, chymotrypsin, and elastase are all serine proteases that cleave after different amino acids. What is responsible for the substrate specificity? Choose one: A. Different amino acids involved in the catalytic triad OB. Each protease is made in a different cell type. C. The substrate binding pockets accommodate different amino acids. D. Different catalytic mechanisms
1.. Example questions to guide you through the mechanism study of Serine proteases Describe substrate binding, including the role and chemical nature of the "specificity pocket" in chymotrypsin, and which peptide bond in the substrate (relative to the specificity group) will be cleaved. Draw the structure of the catalytic triad at the beginning of the reaction, and explain how the states of ionization and hydrogen bonding pattern of those 3 groups change step by step during catalysis. Explain the role...
1. ASP has an important role in hydrogen bonding with the His residue in the catalytic triad of chymotrypsin. ASP and GLU have very similar properties as amino acids. Yet, mutation of ASP to GLU in the traid results in a 10^5 fold decrease in enzyme activity. Why do you think this could be the case?