EC 3.4.23.34 - Cathepsin E

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 3.4.23.34

Names

Accepted name:
cathepsin E
Other names:
EMAP
SMP
cathepsin D-like acid proteinase
cathepsin D-type proteinase
cathepsin E-like acid proteinase
erythrocyte membrane aspartic proteinase
non-pepsin proteinase
slow-moving proteinase
Systematic name:

Reaction

Comments:

Found in stomach, spleen, erythrocyte membrane; not lysosomal. Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or reduction produces monomer. In peptidase family A1 (pepsin A 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
Gene Ontology: GO:0004193
CAS Registry Number: 110910-42-4
UniProtKB/Swiss-Prot:

References

  1. Lapresle, C., Puizdar, V., Porchon-Bertolotto, C., Joukoff, E. and Turk, V.
    Structural differences between rabbit cathepsin E and cathepsin D.
    Biol. Chem. Hoppe-Seyler 367: 523-526 (1986). [PMID: 3741628]
  2. Yonezawa, S., Fujii, K., Maejima, Y., Tamoto, K., Mori, Y. and Muto, N.
    Further studies on rat cathepsin E: subcellular localization and existence of the active subunit form.
    Arch. Biochem. Biophys. 267: 176-183 (1988). [PMID: 3058036]
  3. Jupp, R.A., Richards, A.D., Kay, J., Dunn, B.M., Wyckoff, J.B., Samloff, I.M. and Yamamoto, K.
    Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E.
    Biochem. J. 254: 895-898 (1988). [PMID: 3058118]
  4. Azuma, T., Pals, G., Mohandas, T.K., Couvreur, J.M. and Taggart, R.T.
    Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases.
    J. Biol. Chem. 264: 16748-16753 (1989). [PMID: 2674141]

[EC 3.4.23.34 created 1992]