EC 18.104.22.168 - Phytepsin
IntEnz Enzyme Nomenclature
- Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe┼Asp- and -Asp┼Asp- bonds in 2S albumin from plant seeds.
Known particularly from barley grain, but present in other plants also. In peptidase family A1 (pepsin A family), but structurally distinct in containing an internal region of about 100 amino acids not generally present in the family.
Links to other databases
Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D.Eur. J. Biochem. 202: 1021-1027 (1991). [PMID: 1722454]
Hydrolytic specificity of the barley grain aspartic proteinase.Phytochemistry 32: 799-803 (1993). [PMID: 7763475]
Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases.Eur. J. Biochem. 232: 77-83 (1995). [PMID: 7556174]
Structure and possible function of aspartic proteinases in barley and other plants.Adv. Exp. Med. Biol. 362: 241-254 (1995). [PMID: 8540324]
[EC 22.214.171.124 created 1997]