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Cathepsin e

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Cathepsin E
Identifiers
EC no.3.4.23.34
CAS no.110910-42-4
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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.

References

  1. ^ 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. doi:10.1515/bchm3.1986.367.1.523. PMID 3741628.
  2. ^ 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. doi:10.1016/0003-9861(88)90021-5. PMID 3058036.
  3. ^ 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. PMID 3058118.
  4. ^ 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.

See also