Aspartic peptidase also known as aspartyl proteases () are a widely distributed family of proteolytic enzymes 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 184.108.40.206) and E (EC 220.127.116.11).
- Mammalian renin (EC 18.104.22.168) whose function is to generate angiotensin I from angiotensinogen in the plasma.
- Fungal proteases such as aspergillopepsin A (EC 22.214.171.124) candidapepsin (EC 126.96.36.199) mucoropepsin (EC 188.8.131.52) (mucor rennin) endothiapepsin (EC 184.108.40.206) polyporopepsin (EC 220.127.116.11) and rhizopuspepsin (EC 18.104.22.168).
- Yeast saccharopepsin (EC 22.214.171.124) (proteinase A) (gene PEP4). PEP4 is implicated in posttranslational regulation of vacuolar hydrolases.
- Yeast barrierpepsin (EC 126.96.36.199) (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.
Most retroviruses and some plant viruses such as badnaviruses encode for an aspartyl protease which is an homodimer of a chain of about 95 to 125 amino acids. In most retroviruses the protease is encoded as a segment of a polyprotein which is cleaved during the maturation process of the virus. It is generally part of the pol polyprotein and more rarely of the gag polyprotein.