Cathepsin e
Cathepsin E | |||||||||
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Identifiers | |||||||||
EC number | 3.4.23.34 | ||||||||
CAS number | 110910-42-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Cathepsin E (EC 3.4.23.34, slow-moving proteinase, erythrocyte membrane aspartic proteinase, SMP, EMAP, non-pepsin proteinase, cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Similar to cathepsin D, but slightly broader specificity
This enzyme is found in stomach, spleen, erythrocyte membrane.
See also
References
- ↑ Lapresle, C.; Puizdar, V.; Porchon-Bertolotto, C.; Joukoff, E.; Turk, V. (1986). "Structural differences between rabbit cathepsin E and cathepsin D". Biol. Chem. Hoppe-Seyler. 367: 523–526. PMID 3741628. doi:10.1515/bchm3.1986.367.1.523.
- ↑ Yonezawa, S.; Fujii, K.; Maejima, Y.; Tamoto, K.; Mori, Y.; Muto, N. (1988). "Further studies on rat cathepsin E: subcellular localization and existence of the active subunit form". Arch. Biochem. Biophys. 267: 176–183. PMID 3058036. doi:10.1016/0003-9861(88)90021-5.
- ↑ Jupp, R.A.; Richards, A.D.; Kay, J.; Dunn, B.M.; Wyckoff, J.B.; Samloff, I.M.; Yamamoto, K. (1988). "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. PMC 1135167 . PMID 3058118.
- ↑ Azuma, T.; Pals, G.; Mohandas, T.K.; Couvreur, J.M.; Taggart, R.T. (1989). "Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases". J. Biol. Chem. 264: 16748–16753. PMID 2674141.
External links
- Cathepsin E at the US National Library of Medicine Medical Subject Headings (MeSH)
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