1. Propose a mechanism by which HIV protease hydrolytically cleaves the peptide bond of the substrate shown in the active site. The mechanism you draw requires only two steps containing arrows, you can draw arrows on top of the image shown at left.

Biochemistry
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Chapter1: Biochemistry: An Evolving Science
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## Mechanism of HIV Protease Cleavage

**Objective:** Propose a mechanism by which HIV protease hydrolytically cleaves the peptide bond of the substrate shown in the active site.

### Instructions

1. **Draw 3 Arrows (Step 1):** Illustrate the initial step using three curved arrows to denote the electron flow from the substrate and enzyme.
   
2. **Draw 2 Arrows (Step 2):** Show the subsequent step using two additional arrows to complete the mechanism.

3. **Show Final Products & Enzyme:** Illustrate the final cleaved products and the enzyme after the reaction.

### Diagram Description

- **Active Site Dynamics:** The diagram features a peptide substrate bound to the HIV protease enzyme's active site. Aspartic acids (Asp25) are crucial in the mechanism, depicted interacting with the substrate.
  
- **Chemical Structure:** The peptide structure illustrated includes several key functional groups such as carbonyls and amino groups, relevant for mechanistic understanding.

### Question

- **Between which 2 amino acids is the protease cleavage occurring?**

This educational content is designed to aid in understanding the enzymatic cleavage mechanism by HIV protease, a critical process in its biological function.
Transcribed Image Text:## Mechanism of HIV Protease Cleavage **Objective:** Propose a mechanism by which HIV protease hydrolytically cleaves the peptide bond of the substrate shown in the active site. ### Instructions 1. **Draw 3 Arrows (Step 1):** Illustrate the initial step using three curved arrows to denote the electron flow from the substrate and enzyme. 2. **Draw 2 Arrows (Step 2):** Show the subsequent step using two additional arrows to complete the mechanism. 3. **Show Final Products & Enzyme:** Illustrate the final cleaved products and the enzyme after the reaction. ### Diagram Description - **Active Site Dynamics:** The diagram features a peptide substrate bound to the HIV protease enzyme's active site. Aspartic acids (Asp25) are crucial in the mechanism, depicted interacting with the substrate. - **Chemical Structure:** The peptide structure illustrated includes several key functional groups such as carbonyls and amino groups, relevant for mechanistic understanding. ### Question - **Between which 2 amino acids is the protease cleavage occurring?** This educational content is designed to aid in understanding the enzymatic cleavage mechanism by HIV protease, a critical process in its biological function.
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