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Literature summary for 3.4.22.15 extracted from

  • Yamashita, M.; Konagaya, S.
    Purification and characterization of cathepsin I from the white muscle of chum salmon, Oncorhynchus keta (1990), Comp. Biochem. Physiol. B, 96, 247-252.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol enhances activity Oncorhynchus keta
dithiothreitol enhances activity Oncorhynchus keta
EDTA enhances activity Oncorhynchus keta
thiol-reducing agent required Oncorhynchus keta

Inhibitors

Inhibitors Comment Organism Structure
antipain
-
Oncorhynchus keta
chymostatin
-
Oncorhynchus keta
Cys
-
Oncorhynchus keta
Hg2+ HgCl2 Oncorhynchus keta
iodoacetic acid
-
Oncorhynchus keta
leupeptin
-
Oncorhynchus keta
NEM
-
Oncorhynchus keta
PCMB
-
Oncorhynchus keta
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
Oncorhynchus keta

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00168
-
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
Oncorhynchus keta

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
gel filtration Oncorhynchus keta

Organism

Organism UniProt Comment Textmining
Oncorhynchus keta
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oncorhynchus keta

Source Tissue

Source Tissue Comment Organism Textmining
muscle white muscle Oncorhynchus keta
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Oncorhynchus keta

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
azocasein + H2O
-
Oncorhynchus keta ?
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
-
Oncorhynchus keta ?
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
-
Oncorhynchus keta ?
-
?
Hemoglobin + H2O
-
Oncorhynchus keta ?
-
?
Insulin B-chain + H2O main cleavage sites: Glu13-Ala14 and Tyr26-Thr27, minor cleavage sites: Val2-Asn3, Asn3-Gln4, Cys7-Glu8, Tyr16-Leu17, Leu17-Val18 Oncorhynchus keta ?
-
?
additional information the enzyme has a preference for hydrophobic amino acids in P2 and P3 residues Oncorhynchus keta ?
-
?
serum albumin + H2O
-
Oncorhynchus keta ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 30000, SDS-PAGE Oncorhynchus keta

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
15.8
-
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
Oncorhynchus keta

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6
-
hydrolysis of benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide Oncorhynchus keta

pH Range

pH Minimum pH Maximum Comment Organism
4.2 6.7 pH 4.2: about 50% of maximal activity, pH 6.7: about 35% of maximal activity, hydrolysis of benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide Oncorhynchus keta