EC 3.4.23.40 - Phytepsin

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IntEnz Enzyme Nomenclature
EC 3.4.23.40

Names

Accepted name:
phytepsin
Systematic name:

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00128
Structural data: CSA , EC2PDB
CAS Registry Number: 78169-47-8
UniProtKB/Swiss-Prot:

References

  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: 1021-1027 (1991). [PMID: 1722454]
  2. Kervinen, J., Sarkkinen, P., Kalkkinen, N., Mikola, L. and Saarma, M.
    Hydrolytic specificity of the barley grain aspartic proteinase.
    Phytochemistry 32: 799-803 (1993). [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: 77-83 (1995). [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: 241-254 (1995). [PMID: 8540324]

[EC 3.4.23.40 created 1997]