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Literature summary for 3.4.22.1 extracted from

  • Therrien, C.; Lachance, P.; Sulea, T.; Purisima, E.O.; Qi, H.; Ziomek, E.; Alvarez-Hernandez, A.; Roush, W.R.; Menard, R.
    Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities (2001), Biochemistry, 40, 2702-2711.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
CA074 kinetic analysis Homo sapiens
E64 kinetic analysis Homo sapiens
n-propyl-(2S,3S)-trans-epoxysuccinyl-L-Ile-OH kinetic analysis Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P07858
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-

Reaction

Reaction Comment Organism Reaction ID
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides kinetics Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme prefers dipeptidyl pathway over monopeptidyl carboxypeptidase pathway Homo sapiens ?
-
?