Aspartic peptidase, also known as aspartyl proteases (3.4.23.-) are a widely distributed family of proteolytic enzymes [1, 2, 3] known to exist in vertebrates, fungi, plants, retroviruses and some plant viruses. Aspartate proteases of eukaryotes are monomeric enzymes which consist of two domains. Each domain contains an active site centered on a catalytic aspartyl residue. The two domains most probably evolved from the duplication of an ancestral gene encoding a primordial domain. Currently known eukaryotic aspartyl proteases are:

• Vertebrate gastric pepsins A and C (also known as gastricsin). Vertebrate chymosin (rennin), involved in digestion and used for making cheese.
• Vertebrate lysosomal cathepsins D (EC 3.4.23.5) and E (EC 3.4.23.34).
• Mammalian renin (EC 3.4.23.15) whose function is to generate angiotensin I from angiotensinogen in the plasma.
• Fungal proteases such as aspergillopepsin A (EC 3.4.23.18), candidapepsin (EC 3.4.23.24), mucoropepsin (EC 3.4.23.23) (mucor rennin), endothiapepsin (EC 3.4.23.22), polyporopepsin (EC 3.4.23.29), and rhizopuspepsin (EC 3.4.23.21).
• Yeast saccharopepsin (EC 3.4.23.25) (proteinase A) (gene PEP4). PEP4 is implicated in posttranslational regulation of vacuolar hydrolases.
• Yeast barrierpepsin (EC 3.4.23.35) (gene BAR1); a protease that cleaves alpha-factor and thus acts as an antagonist of the mating pheromone.
• Fission yeast sxa1 which is involved in degrading or processing the mating pheromones.

This signature contains the active site residues which are conserved in eukaryotic and viral aspartyl proteases.

1. Gastric proteinases--structure, function, evolution and mechanism of action. null 17, 52-84
2. The structure and function of the aspartic proteinases. Biochemistry 19, 189-215
3. Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases. Essays Biochem. 30, 4663-71

Aspartic peptidase, also known as aspartyl proteases (Show more...

Download genes (select columns to include)