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
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
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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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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