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Literature summary for 3.4.22.38 extracted from

  • Godat, E.; Lecaille, F.; Desmazes, C.; Duchene, S.; Weidauer, E.; Saftig, P.; Broemme, D.; Vandier, C.; Lalmanach, G.
    Cathepsin K: a cysteine protease with unique kinin-degrading properties (2004), Biochem. J., 383, 501-506.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.38

Protein Variants

Protein Variants Comment Organism
Y67L/L205A 2-aminobenzoyl-RP-PGFSPFR-(3-nitrotyrosine) is not cleaved by the the mutant enzyme Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
kinin + H2O Mus musculus the potency of cathepsin K to modulate bradikinin-dependent contraction of smooth muscles, cathepsin K may act as a kininase ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminobenzoyl-RPPGFSPFR-(3-nitrotyrosine) + H2O
-
 Mus musculus ?
-
 ?
bradykinin + H2O
-
 Mus musculus bradykinin(1-4) + bradykinin(5-9)
-
 ?
kinin + H2O the potency of cathepsin K to modulate bradikinin-dependent contraction of smooth muscles, cathepsin K may act as a kininase Mus musculus ?
-
 ?
kinin + H2O cleavage at the Gly4 Β–Phe5 bond Mus musculus ?
-
 ?
additional information 2-aminobenzoyl-RP-PGFSPFR-(3-nitrotyrosine) is not cleaved by the mutant enzyme Y67L/L205A Mus musculus ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7.4 kcat/Km with 2-aminobenzoyl-RPPGFSPFR-(3-nitrotyrosine) is 1.4fold higher at pH 6.0 than at pH 7.4 Mus musculus