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Literature summary for 3.4.22.1 extracted from

  • Pungercar, J.R.; Caglic, D.; Sajid, M.; Dolinar, M.; Vasiljeva, O.; Pozgan, U.; Turk, D.; Bogyo, M.; Turk, V.; Turk, B.
    Autocatalytic processing of procathepsin B is triggered by proenzyme activity (2009), FEBS J., 276, 660-668.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information the autocatalytic processing of procathepsin B is triggered by proenzyme activity, overview Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of recombinant human procathepsin B and cathepsin B in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
K39A/R40A site-directed mutagenesis, the mutant procathepsin B performs autocatalytic activation 2fold faster compared to the wild-type variant Homo sapiens
L41A site-directed mutagenesis, the mutant procathepsin B performs autocatalytic activation 2fold faster compared to the wild-type variant Homo sapiens
additional information autocatalytic activation of procathepsin B is largely insensitive to mutations in the cleavage site region Homo sapiens
R40A site-directed mutagenesis, the mutant procathepsin B performs autocatalytic activation 2fold faster compared to wild-type variant Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
DCG-04 an E-64-type inhibitor, inhibits both mature cathepsin B and its zymogen 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 procathepsin B is largely insensitive to mutations in the cleavage site region and can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the autocatalytic processing of procathepsin B is triggered by proenzyme activity, overview Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information autocatalytic activation of procathepsin B is largely insensitive to mutations in the cleavage site region and can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins Homo sapiens ?
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?
additional information procathepsin B shows autocatalytic processing triggered by proenzyme activity, identification of cleavage sites and initiation mechanism, overview. A multi-step process, starting with a unimolecular conformational change of the zymogen, which unmasks the active site and, in the presence of negatively charged molecules and/or surfaces, also converts the zymogen into a better substrate, followed by the bimolecular proteolytic removal of the propeptide Homo sapiens ?
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?
N-benzyloxycarbonyl-L-arginyl-L-arginyl-4-methylcoumarin 7-amide + H2O substrate of mature cathepsin B, also procathepsin B is catalytically active on the synthetic substrate but to a lower extent. The unfolded proenzymeis inactive Homo sapiens N-benzyloxycarbonyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
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Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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hydrolytic enzyme assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
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in vitro autocatalytic processing of procathepsin B Homo sapiens
7.6
-
hydrolytic enzyme assay at Homo sapiens

General Information

General Information Comment Organism
physiological function autocatalytic activation of procathepsin B can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins Homo sapiens