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Phytepsin (EC 3.4.23.40) is an enzyme. 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. It is an aspartic protease with a plant-specific insert.

References

1. Runeberg-Roos P, Törmäkangas K, Ostman A (December 1991). "Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D". European Journal of Biochemistry. 202 (3): 1021–7. doi:10.1111/j.1432-1033.1991.tb16465.x. PMID 1722454.
2. Kervinen J, Sarkkinen P, Kalkkinen N, Mikola L, Saarma M (March 1993). "Hydrolytic specificity of the barley grain aspartic proteinase". Phytochemistry. 32 (4): 799–803. doi:10.1016/0031-9422(93)85208-9. PMID 7763475.
3. Asakura T, Watanabe H, Abe K, Arai S (August 1995). "Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases". European Journal of Biochemistry. 232 (1): 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, Teeri TH (1995). "Structure and possible function of aspartic proteinases in barley and other plants". Advances in Experimental Medicine and Biology. 362: 241–54. doi:10.1007/978-1-4615-1871-6_28. ISBN 978-1-4613-5761-2. PMID 8540324. {{cite journal}}: Cite journal requires |journal= (help)

External links

• Phytepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

• Biology

• EC 3.4.23