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
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**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.
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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