Reaction: Similar to cathepsin D, but slightly broader specificity
Other names: 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, MEROPS, Metacyc, PDB, CAS registry number: 110910-42-4
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 (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]