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In step four of proteolytic cleavage via chymotrypsin, water is introduced into the active site. Label on the image below what catalytic mechanisms are depicted to enhance the overall rate of catalysis . CH2 Ser 195- CH,-0 His IN- 57 Н. Asp 102 ACYL-ENZYME- H,0 COMPLEX

In step four of proteolytic cleavage via chymotrypsin, water is introduced into the active site. Label on the image below what catalytic mechanisms are depicted to enhance the overall rate of catalysis . CH2 Ser 195- CH,-0 His IN- 57 Н. Asp 102 ACYL-ENZYME- H,0 COMPLEX

Biochemistry
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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In step four of proteolytic cleavage via chymotrypsin, water is introduced into the active site. Label on the image below what catalytic mechanisms are depicted to enhance the overall rate of catalysis. ### Diagram Explanation The diagram shows the acyl-enzyme complex with a water molecule introduced, highlighting the catalytic triad of chymotrypsin: - **Ser 195 (Serine 195)**: Positioned in a yellow oval, it plays a crucial role in the mechanism by forming a covalent bond with the substrate (depicted with a line pointing towards the CH₂-O group). - **His 57 (Histidine 57)**: Shown in a blue oval, this amino acid acts as a general base in the triad, facilitating proton transfer (noted with the N-containing imidazole ring). - **Asp 102 (Aspartate 102)**: Presented in an orange oval, it stabilizes histidine and is crucial for proper alignment in the catalytic mechanism. The interaction between these residues, along with the presence of the water molecule, is essential for the catalytic function of chymotrypsin, enhancing the overall rate of cleavage. The labels and arrows in the diagram point to these components, illustrating their roles and interactions.
Transcribed Image Text:In step four of proteolytic cleavage via chymotrypsin, water is introduced into the active site. Label on the image below what catalytic mechanisms are depicted to enhance the overall rate of catalysis. ### Diagram Explanation The diagram shows the acyl-enzyme complex with a water molecule introduced, highlighting the catalytic triad of chymotrypsin: - **Ser 195 (Serine 195)**: Positioned in a yellow oval, it plays a crucial role in the mechanism by forming a covalent bond with the substrate (depicted with a line pointing towards the CH₂-O group). - **His 57 (Histidine 57)**: Shown in a blue oval, this amino acid acts as a general base in the triad, facilitating proton transfer (noted with the N-containing imidazole ring). - **Asp 102 (Aspartate 102)**: Presented in an orange oval, it stabilizes histidine and is crucial for proper alignment in the catalytic mechanism. The interaction between these residues, along with the presence of the water molecule, is essential for the catalytic function of chymotrypsin, enhancing the overall rate of cleavage. The labels and arrows in the diagram point to these components, illustrating their roles and interactions.
Expert Solution
Step 1

Chymotrypsin is synthesized by the pancreas in an inactive form, called as chymotrypsinogen. It is a proteolytic enzyme. This enzyme helps in the hydrolysis of the peptide bond. Chymotrypsin also help in hydrolysis of the ester bond. It is a serine protease. Its active site consists of the serine residue.  

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