Aspartic Protease ()

Aspartic Protease Overview

Aspartic proteases are a class of proteolytic enzymes that utilize two highly conserved aspartic acid residues in their active site to catalyze the hydrolysis of peptide bonds in proteins. They are found across a wide range of organisms, including fungi, plants, animals, and viruses. They play diverse roles in biological processes such as protein digestion, blood pressure regulation, and intracellular protein degradation. Dysregulation or pathogenic activity of specific members makes them important drug targets.

Mechanism of Action

Inhibition of protease activity by binding to the active site and preventing substrate binding.

Biological Functions

Safety Considerations

Interacting Drugs