The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: cathepsin E
Reaction: Similar to cathepsin D, but slightly broader specificity
Other name(s): slow-moving proteinase; erythrocyte membrane aspartic proteinase; SMP; erythrocyte membrane aspartic proteinase; EMAP; non-pepsin proteinase; cathepsin D-like acid proteinase; cathepsin E-like acid proteinase; cathepsin D-type proteinase
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: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 110910-42-4
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 (1986) 523–526. [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 (1988) 176–183. [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 (1988) 895–898. [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 (1989) 16748–16753. [PMID: 2674141]
[EC created 1992]

Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald