Enzyme Results

22 enzymatic activities found for "cathepsin"

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Enzyme Family
  • Hydrolases (20)
  • Transferases (1)
  • Oxidoreductases (1)
Name Alternative Names Protein Hits Enzyme Family EC Catalytic Activity Cofactor
Cathepsin V
  • Cathepsin L2.
  • Cathepsin U.
4 Hydrolases 3.4.22.43 [The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) andsynthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec).]
Cathepsin B
  • Cathepsin B1.
14 Hydrolases 3.4.22.1 [Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates(thus differing from cathepsin L). In addition to being an endopeptidase,shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.]
Cathepsin S
3 Hydrolases 3.4.22.27 [Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec,and more activity on the Z-Val-Val-Arg-|-Xaa compound.]
Cathepsin L
39 Hydrolases 3.4.22.15 [Specificity close to that of papain. As compared to cathepsin B,cathepsin L exhibits higher activity toward protein substrates, but haslittle activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.]
Cathepsin H
  • Aleurain.
  • Cathepsin BA.
  • Cathepsin B3.
  • N-benzoylarginine-beta-naphthylamide hydrolase.
10 Hydrolases 3.4.22.16 [Hydrolysis of proteins, acting as an aminopeptidase (notably, cleavingArg-|-Xaa bonds) as well as an endopeptidase.]
Cathepsin K
  • Cathepsin O.
  • Cathepsin X.
  • Cathepsin O2.
1 Hydrolases 3.4.22.38 [Broad proteolytic activity. With small-molecule substrates andinhibitors, the major determinant of specificity is P2, which ispreferably Leu, Met > Phe, and not Arg.]
Cathepsin E
  • Slow-moving proteinase.
  • Erythrocyte membrane aspartic proteinase.
5 Hydrolases 3.4.23.34 [Similar to cathepsin D, but slightly broader specificity.]
Cathepsin X
  • Cysteine-type carboxypeptidase.
  • Acid carboxypeptidase.
  • Cathepsin IV.
  • Cathepsin Z.
  • Cathepsin B(2).
  • Lysosomal carboxypeptidase B.
2 Hydrolases 3.4.18.1 [Release of C-terminal amino acid residues with broad specificity,but lacks action on C-terminal proline. Shows weak endopeptidaseactivity.]
Cathepsin F
3 Hydrolases 3.4.22.41 [The recombinant enzyme cleaves synthetic substrates with Phe and Leu(better than Val) in P2, with high specificity constant (k(cat)/K(m))comparable to that of cathepsin L.]
Cathepsin G
2 Hydrolases 3.4.21.20 [Specificity similar to chymotrypsin C.]