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Literature summary extracted from
- Role of loop structures of neuropsin in the activity of serine protease and regulated secretion (2002), J. Biol. Chem., 277, 14724-14730.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.21.118 | expression and secretion of wild-type and mutants from Neuro2a cells | Mus musculus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.21.118 | C108S | oligonucleotide-directed mutagenesis, reduced Km, increased kcat, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | Mus musculus |
| 3.4.21.118 | C145S | oligonucleotide-directed mutagenesis of disulfide bond SS3, reduced Km and kcat, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | Mus musculus |
| 3.4.21.118 | C208S | oligonucleotide-directed mutagenesis of disulfide bond SS6, highly reduced Km and reduced kcat, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | Mus musculus |
| 3.4.21.118 | C233S | oligonucleotide-directed mutagenesis, highly reduced Km and slightly reduced kcat, reduced activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | Mus musculus |
| 3.4.21.118 | C246S | oligonucleotide-directed mutagenesis, reduced Km and kcat, decreased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | Mus musculus |
| 3.4.21.118 | C39S | oligonucleotide-directed mutagenesis of disulfide bond SS1, increased Km, reduced kcat, reduced activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | Mus musculus |
| 3.4.21.118 | C7S | oligonucleotide-directed mutagenesis, reduced Km and kcat, slightly decreased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | Mus musculus |
| 3.4.21.118 | D206V | oligonucleotide-directed mutagenesis, reduced Km and highly reduced kcat, decreased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-7-amino-4-methylcoumarin | Mus musculus |
| 3.4.21.118 | additional information | additional deletion N113-E115 in mutant N110S: decreased kcat and Km, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | Mus musculus |
| 3.4.21.118 | N110A | oligonucleotide-directed mutagenesis, reduced Km and kcat, slightly increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | Mus musculus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.21.118 | 0.22 | - |
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide | recombinant wild-type enzyme, pH 8.0, 25°C | Mus musculus |  |
| 3.4.21.118 | 0.28 | - |
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | recombinant wild-type enzyme, pH 8.0, 25°C | Mus musculus | |
| 3.4.21.118 | 0.32 | - |
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide | recombinant wild-type enzyme, pH 8.0, 25°C | Mus musculus | |
| 3.4.21.118 | 8.36 | - |
Pro-Phe-Arg-4-methylcoumaryl-7-amide | recombinant wild-type enzyme, pH 8.0, 25°C | Mus musculus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.118 | extracellular | secreted | Mus musculus | - |
- |
| 3.4.21.118 | extracellular | disruption of loop C and the kallikrein loop enhances the regulated secretion, no loop disruption does lead to inhibition of secretion | Mus musculus | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.118 | polypeptide + H2O | Mus musculus | - |
peptides | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.118 | Mus musculus | Q61955 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.21.118 | glycoprotein | N-glycosylated at the kallikrein loop, residues His91-Ile103, oligosacchride chain is essential for activity | Mus musculus |
| 3.4.21.118 | proteolytic modification | recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus | Mus musculus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.21.118 | brain | - |
Mus musculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.118 | additional information | recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus | Mus musculus | ? | - |
? | |
| 3.4.21.118 | additional information | loop C and the N-linked oligosaccharide chain on the kallikrein loop affect the catalytic efficiency and P2 specificity, respectively | Mus musculus | ? | - |
? | |
| 3.4.21.118 | additional information | disulfide bonds SS1 in loop E, Gly142-Leu155, and SS6 in loop G, Ser185-Gly197, are essential for catalytic activity | Mus musculus | ? | - |
? | |
| 3.4.21.118 | polypeptide + H2O | - |
Mus musculus | peptides | - |
? | |
| 3.4.21.118 | Pro-Phe-Arg-4-methylcoumaryl-7-amide | recombinant wild-type and mutants | Mus musculus | Pro-Phe-Arg + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.21.118 | tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide + H2O | wild-type and mutants | Mus musculus | tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.21.118 | tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O | recombinant wild-type and mutants | Mus musculus | tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.21.118 | tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O | best substrate | Mus musculus | tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.21.118 | tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O | recombinant wild-type and mutants | Mus musculus | tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.118 | More | determination of loop structure and organization | Mus musculus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.118 | 25 | - |
assay at | Mus musculus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.21.118 | 31.3 | - |
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide | recombinant wild-type enzyme, pH 8.0, 25°C | Mus musculus | |
| 3.4.21.118 | 34.8 | - |
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide | recombinant wild-type enzyme, pH 8.0, 25°C | Mus musculus | |
| 3.4.21.118 | 100 | - |
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide | recombinant wild-type enzyme, pH 8.0, 25°C | Mus musculus | |
| 3.4.21.118 | 193 | - |
Pro-Phe-Arg-4-methylcoumaryl-7-amide | recombinant wild-type enzyme, pH 8.0, 25°C | Mus musculus | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.118 | 8 | - |
assay at | Mus musculus |
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