3. Compare and contrast how thiolase and chymotrypsin creates and stabilizes its intermediates.
3. Compare and contrast how thiolase and chymotrypsin creates and stabilizes its intermediates.
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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Question

Transcribed Image Text:**Diagram Explanation:**
The diagram illustrates a chemical structure involved in enzymatic activity. It depicts a molecule with several key functional groups:
- A carbon chain connected to an "R" group, which represents a variable side chain.
- A negatively charged oxygen atom bonded to a carbon.
- A sulfur-containing group attached to Coenzyme A (CoA), indicating the presence of a thioester bond.
- A ring structure resembling a pyrrole, marked with NH groups, and another aromatic ring suggesting an indole ring.
- Additional CH2 groups connecting sections of the molecule.
**Text Explanation:**
3. Compare and contrast how thiolase and chymotrypsin create and stabilize their intermediates.
**Discussion Points:**
- **Thiolase:**
- Involves catalytic mechanisms typically forming thioester intermediates.
- Stabilizes intermediates through interactions with CoA and side chain groups.
- **Chymotrypsin:**
- A serine protease that stabilizes its tetrahedral intermediates through an oxyanion hole.
- Utilizes a catalytic triad for processing peptide bonds.
The comparison explores the mechanistic differences between these enzymes in intermediate formation and stabilization.
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