Aspartic proteases

Aspartic proteases (pronunciation: as-par-tic pro-tea-ses) are a category of protease enzymes that use an aspartate residue for catalytic activity. They are found in a wide variety of organisms, from viruses to humans, and play a crucial role in many biological processes.

Etymology

The term "Aspartic proteases" is derived from the word "aspartate", a type of amino acid, and "protease", an enzyme that conducts proteolysis - the breakdown of proteins into smaller polypeptides or single amino acids.

Function

Aspartic proteases are involved in a variety of biological processes, including digestion, immune response, and apoptosis. They function by using a water molecule to cleave the peptide bond, a process known as hydrolysis. This is facilitated by two aspartate residues in the active site of the enzyme.

Types

There are two main types of aspartic proteases: those found in the stomach, such as pepsin and cathepsin, and those found in retroviruses, such as HIV protease. Each type has a unique structure and function.

Clinical Significance

Aspartic proteases are of significant clinical interest due to their role in disease processes. For example, the HIV protease is a key target for antiretroviral therapy in the treatment of HIV/AIDS. In addition, mutations in the genes encoding aspartic proteases can lead to diseases such as gaucher's disease and congenital adrenal hyperplasia.

See Also

• Protease
• Aspartate
• Proteolysis
• Pepsin
• Cathepsin
• HIV protease
• Antiretroviral therapy
• Gaucher's disease
• Congenital adrenal hyperplasia

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