EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.22.B65 | 7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O |
- |
Rattus norvegicus |
7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-Dap(Dnp)-Ala-Arg-NH2 |
- |
? |
| 3.4.22.B65 | 7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O |
- |
Mus musculus |
7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-Dap(Dnp)-Ala-Arg-NH2 |
- |
? |
| 3.4.22.B65 | azocasein + H2O |
- |
Mus musculus |
? |
- |
? |
| 3.4.22.B65 | calreticulin + H2O |
endoplasmic reticulum protein substrate identified by incubation of recombinant enzyme with rat choriocarcinoma cell proteins |
Mus musculus |
? |
protein is processed from the C-terminus, with removal of the KDEL endoplasmic reticulum retention signal. Cathepsin L co-localizes with calreticulin in rat choriocarcinoma cell |
? |
| 3.4.22.B65 | Gp96 protein + H2O |
endoplasmic reticulum protein substrate identified by incubation of recombinant enzyme with rat choriocarcinoma cell proteins |
Mus musculus |
? |
protein is sequentially processed by cathepsin P at 2 sites towards the C-terminus of the protein, with removal of the KDEL endoplasmic reticulum retention signal. Cathepsin L co-localizes with gp96 in rat choriocarcinoma cell |
? |
| 3.4.22.B65 | more |
no substrates: Z-Phe-Arg-NHMec, Z-Arg-Arg-NHMec, Arg-NHMec, Bz-Phe-Val-Arg-NHMec, succinyl-Ala-Ala-Phe-NHMec, Z-Val-Ala-Asp-NHMec, bradykinin, somatostatin, Fmoc-Tyr-Ala-OH, Z-Gly-Gly-OH, Z-Leu-Tyr-OH, Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2, Mca-Pro-Leu-Ala-Gln-Ala-Val-Dpa-Arg-Ser-Ser-Ser-Arg-NH2 or Dnp-Pro-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(Nma)NH2 |
Mus musculus |
? |
- |
? |
| 3.4.22.B65 | more |
peptides with hydrophobic residues such as Phe, Met, and Leu in the P1 position are preferred substrates of cathepsin P. Substrates with negatively charged amino acids such as Glu, polar uncharged amino acids such as Asn, Gln, Ser, and Thr, and positively charged amino acids such as Arg, Lys, and His in this position are poorly hydrolyzed by cathepsin P due to either reduced kcat or increased Km, or both |
Mus musculus |
? |
- |
? |
| 3.4.22.B65 | o-aminobenzoic acid-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O |
- |
Mus musculus |
o-aminobenzoic acid-ALR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine |
- |
? |
| 3.4.22.B65 | o-aminobenzoic acid-EIFVFKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O |
ideal substrate constructed after analysis of substrate preferences. In contrast to most substrates, hydrolysis is not stimulated by addition of salts |
Mus musculus |
o-aminobenzoic acid-EIF + VFKQ-N-(2,4-dinitrophenyl)ethylenediamine |
- |
? |
| 3.4.22.B65 | o-aminobenzoic acid-ELRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O |
- |
Mus musculus |
o-aminobenzoic acid-ELR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine |
- |
? |
