Phytepsin

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Phytepsin
Identifiers
EC no. 3.4.23.40
CAS no. 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
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PMC articles
PubMed articles
NCBI proteins
Phytepsin
Identifiers
Symbolphytepsin
InterPro IPR033869
CDD cd06098

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. 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. Bibcode:1993PChem..32..799K. 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". Aspartic Proteinases. Advances in Experimental Medicine and Biology. Vol. 362. pp. 241–54. doi:10.1007/978-1-4615-1871-6_28. ISBN   978-1-4613-5761-2. PMID   8540324.
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