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

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.; Östman, A. (1991). "Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D". Eur. J. Biochem. 202 (3): 1021–1027. doi:10.1111/j.1432-1033.1991.tb16465.x. PMID 1722454.
  2. ↑ Kervinen, J.; Sarkkinen, P.; Kalkkinen, N.; Mikola, L.; Saarma, M. (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. (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 (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, T.H. (1995). "Structure and possible function of aspartic proteinases in barley and other plants". Adv. Exp. Med. Biol. Advances in Experimental Medicine and Biology. 362: 241–254. doi:10.1007/978-1-4615-1871-6_28. ISBN 978-1-4613-5761-2. PMID 8540324.
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