The HIV protease enzyme uses a general acid-base catalysis mechanism to cleave viral polypeptides but does not use a covalent catalysis. This enzyme functions optimally in the pH range of 4-6. Due to the specific amino acids involved in this catalysis, HIV protease is a member of which subclass of proteases?

Question

Quizplus · Accepted Answer

The specific amino acids involved in the catalytic mechanism of the HIV protease enzyme suggest it is an aspartyl protease. Aspartyl proteases use a similar mechanism to serine proteases but have two aspartic acid residues in their active site instead of a serine and a histidine. Additionally, the optimal pH range for the HIV protease aligns with the optimal pH range for aspartyl proteases, which is typically around 3-5. Metalloproteases use metal ions in their catalytic mechanism, while serine proteases use a serine residue in their active site with a histidine residue. Cysteine proteases and lysine proteases have a thiolate or lysine residue, respectively, in their active site.

The HIV Protease Enzyme Uses a General Acid-Base Catalysis Mechanism