Entry |
|
Name |
cathepsin E;
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
|
Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
 |
Reaction(IUBMB) |
Similar to cathepsin D, but slightly broader specificity
|
Comment |
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)
|
History |
EC 3.4.23.34 created 1992
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Orthology |
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Genes |
» show all
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Reference |
|
Authors |
Lapresle C, Puizdar V, Porchon-Bertolotto C, Joukoff E, Turk V. |
Title |
Structural differences between rabbit cathepsin E and cathepsin D. |
Journal |
Biol. Chem. Hoppe. Seyler. 367 (1986) 523-6. |
Reference |
|
Authors |
Yonezawa S, Fujii K, Maejima Y, Tamoto K, Mori Y, Muto N. |
Title |
Further studies on rat cathepsin E: subcellular localization and existence of the active subunit form. |
Journal |
Arch. Biochem. Biophys. 267 (1988) 176-83. |
Reference |
|
Authors |
Jupp RA, Richards AD, Kay J, Dunn BM, Wyckoff JB, Samloff IM, Yamamoto K. |
Title |
Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E. |
Journal |
Biochem. J. 254 (1988) 895-8. |
Reference |
|
Authors |
Azuma T, Pals G, Mohandas TK, Couvreur JM, Taggart RT. |
Title |
Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases. |
Journal |
J. Biol. Chem. 264 (1989) 16748-53. |
Sequence |
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Other DBs |
ExPASy - ENZYME nomenclature database: | 3.4.23.34 |
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