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Literature summary for 3.4.22.1 extracted from

  • Redzynia, I.; Ljunggren, A.; Abrahamson, M.; Mort, J.S.; Krupa, J.C.; Jaskolski, M.; Bujacz, G.
    Displacement of the occluding loop by the parasite protein, chagasin, results in efficient inhibition of human cathepsin B (2008), J. Biol. Chem., 283, 22815-22825.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of mutants as inactive pro-proteins in Pichia pastoris Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified wild-type enzyme and enzyme mutants in complex with inhibitor chagasin, hanging drop vapor diffusion method at 18°C, for crystal form I: mixing of 0.001 ml of 5 mg/ml chagasin solution with 0.002 ml of protein solution containing 3 mg/ml cathepsin B, and 0.002 ml of precipitant solution containing 0.2 M NH4H2PO4, 20% PEG 3350, pH 4.6, 2 weeks, for crystal form II: mixing of 0.001 mL of 5 mg/ml chagasin solution with 0.0015 ml of protein solution containing 3 mg/ml cathepsin B, and 0.001 ml of precipitant solution containing 0.14 M NH4F, 14% PEG 3350, pH 6.2, 1 week, X-ray diffraction structure determination and analysis at 1.8-2.7 A resolution Homo sapiens

Protein Variants

Protein Variants Comment Organism
C29A inactive mutant Homo sapiens
C29A/H110A/S115A an inactive, non-glycosylated cathepsin B mutant Homo sapiens
H110A/S115A a non-glycosylated cathepsin B mutant Homo sapiens
S115A a non-glycosylated cathepsin B mutant Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
chagasin an inhibitor from Trypanosoma cruzi, Three residues from chagasin, Leu65, Gly66, and Ala67, interact with cathepsin B residues Gly74, Gly73, and Asn72, binding mode and structure of wild-type enzyme and non-glycosylated S115A and H110A/S115A cathepsin B mutants, modeling, overview Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.055
-
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin pH 6.5, recombinant enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens autocatalytic activation of the inactive proenzyme ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein glycosylation at Ser115 Homo sapiens
proteolytic modification autocatalytic activation of the purified proenzyme in 20 mM sodium acetate, pH 5.0, 1mM EDTA, for 5 days Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carbobenzoxy-Phe-Ala-Arg-7-amido-4-methylcoumarin + H2O a fluorogenic substrate Homo sapiens carbobenzoxy-Phe-Ala-Arg + 7-amino-4-methylcoumarin
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O a fluorogenic substrate Homo sapiens carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
-
?
additional information autocatalytic activation of the inactive proenzyme Homo sapiens ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
autocatalytic assay at Homo sapiens
6.5
-
enzyme assay at, substrate carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin Homo sapiens