Phytepsin

Phytepsin
Identifiers
EC number	3.4.23.40
CAS number	219715-98-7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

Phytepsin (EC 3.4.23.40) is an enzyme.^[1][2][3][4] This enzyme catalyses the following chemical 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

This enzyme is present in barley grain and other plants.

References

1. Runeberg-Roos, P., Törmäkangas, K. and Östman, A. (1991). "Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D". Eur. J. Biochem. 202: 1021–1027. doi:10.1111/j.1432-1033.1991.tb16465.x. PMID 1722454.
2. Kervinen, J., Sarkkinen, P., Kalkkinen, N., Mikola, L. and Saarma, M. (1993). "Hydrolytic specificity of the barley grain aspartic proteinase". Phytochemistry 32: 799–803. doi:10.1016/0031-9422(93)85208-9. PMID 7763475.
3. Asakura, T., Watanabe, H., Abe, K. and Arai, S. (1995). "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. doi:10.1111/j.1432-1033.1995.tb20783.x. PMID 7556174.
4. Kervinen, J., Törmäkangas, K., Runeberg-Roos, P., Guruprasad, K., Blundell, T. and Teeri, T.H. (1995). "Structure and possible function of aspartic proteinases in barley and other plants". Adv. Exp. Med. Biol. 362: 241–254. doi:10.1007/978-1-4615-1871-6_28. PMID 8540324.

External links

• Phytepsin at the US National Library of Medicine Medical Subject Headings (MeSH)