16. This figure from Foundations should look familiar. Which protein is shown here? catalytic triad A) Aglycosidase B) AG-protein C) Chymotrypsin D) Hexokinase Ser 195 E) Trypsin His 57 Gly 193 N-H N- N-H R N Ca CB R' Asp 102 17. What kind of enzymatic mechanism is shown in this figure from Foundations? A) Specific acid-base catalysis with His57 as the base B) Specific acid-base catalysis with Ser195 as the base C) General acid-base catalysis with Ser195 as the base D) General acid-base catalysis with His57 as the base E) Metal ion catalysis N-H Z-I

Biochemistry
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Chapter1: Biochemistry: An Evolving Science
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**Figure Analysis and Explanation**

**16. Protein Identification**
The figure depicts the catalytic triad found in serine proteases, such as chymotrypsin or trypsin. The question asks which protein is shown:

- **Options:**
  - A) A glycosidase
  - B) A G-protein
  - C) Chymotrypsin
  - D) Hexokinase
  - E) Trypsin

Given the presence of the triad (Ser 195, His 57, Asp 102), the protein is likely a serine protease, such as chymotrypsin or trypsin.

**Diagram Explanation:**
The diagram illustrates a catalytic triad, common in the active sites of serine proteases. The amino acids involved include:
- **Serine (Ser 195)**: A serine residue plays a crucial role in the reaction mechanism, acting as a nucleophile.
- **Histidine (His 57)**: This residue facilitates the nucleophilic attack by deprotonating the serine.
- **Aspartate (Asp 102)**: Stabilizes the positive charge on histidine during the reaction.

**17. Enzymatic Mechanism**
The diagram shows a typical mechanism of general acid-base catalysis involving His 57 and Ser 195.

- **Options:**
  - A) Specific acid-base catalysis with His57 as the base
  - B) Specific acid-base catalysis with Ser195 as the base
  - C) General acid-base catalysis with Ser195 as the base
  - D) General acid-base catalysis with His57 as the base
  - E) Metal ion catalysis

The mechanism depicted is likely D, "General acid-base catalysis with His57 as the base," because the histidine residue acts as a base to deprotonate the serine, allowing it to perform nucleophilic attacks.
Transcribed Image Text:**Figure Analysis and Explanation** **16. Protein Identification** The figure depicts the catalytic triad found in serine proteases, such as chymotrypsin or trypsin. The question asks which protein is shown: - **Options:** - A) A glycosidase - B) A G-protein - C) Chymotrypsin - D) Hexokinase - E) Trypsin Given the presence of the triad (Ser 195, His 57, Asp 102), the protein is likely a serine protease, such as chymotrypsin or trypsin. **Diagram Explanation:** The diagram illustrates a catalytic triad, common in the active sites of serine proteases. The amino acids involved include: - **Serine (Ser 195)**: A serine residue plays a crucial role in the reaction mechanism, acting as a nucleophile. - **Histidine (His 57)**: This residue facilitates the nucleophilic attack by deprotonating the serine. - **Aspartate (Asp 102)**: Stabilizes the positive charge on histidine during the reaction. **17. Enzymatic Mechanism** The diagram shows a typical mechanism of general acid-base catalysis involving His 57 and Ser 195. - **Options:** - A) Specific acid-base catalysis with His57 as the base - B) Specific acid-base catalysis with Ser195 as the base - C) General acid-base catalysis with Ser195 as the base - D) General acid-base catalysis with His57 as the base - E) Metal ion catalysis The mechanism depicted is likely D, "General acid-base catalysis with His57 as the base," because the histidine residue acts as a base to deprotonate the serine, allowing it to perform nucleophilic attacks.
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