The Enzyme Database

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Accepted name: phytepsin
Reaction: 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
Comments: 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: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 219715-98-7
1.  Runeberg-Roos, P., Törmäkangas, K. and Östman, A. Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D. Eur. J. Biochem. 202 (1991) 1021–1027. [DOI] [PMID: 1722454]
2.  Kervinen, J., Sarkkinen, P., Kalkkinen, N., Mikola, L. and Saarma, M. Hydrolytic specificity of the barley grain aspartic proteinase. Phytochemistry 32 (1993) 799–803. [DOI] [PMID: 7763475]
3.  Asakura, T., Watanabe, H., Abe, K. and Arai, S. 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 (1995) 77–83. [DOI] [PMID: 7556174]
4.  Kervinen, J., Törmäkangas, K., Runeberg-Roos, P., Guruprasad, K., Blundell, T. and Teeri, T.H. Structure and possible function of aspartic proteinases in barley and other plants. Adv. Exp. Med. Biol. 362 (1995) 241–254. [PMID: 8540324]
[EC created 1997]

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