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Literature summary extracted from
- Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of endopeptidases (1998), FEBS Lett., 441, 361-365.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.22.34 | transient expression under control of the CMV promotor of wild-type and mutant enzymes in human embryonic kidney HEK 293 cells, all recombinant enzymes are processed normally | Mus musculus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.22.34 | C191S | site-directedd mutagenesis, completely inactive | Mus musculus |
| 3.4.22.34 | C52S | site-directed mutagenesis, as active as the wild-type | Mus musculus |
| 3.4.22.34 | H150A | site-directed mutagenesis, adaptation of the mouse sequence to the human one by introduction of a silent mutation A152S, 4fold less effective expressionin HEK 293 cells compared to wild-type, completely inactive | Mus musculus |
| 3.4.22.34 | H164A | site-directed mutagenesis, control mutant, as active as the wild-type | Mus musculus |
| 3.4.22.34 | H47A | site-directed mutagenesis, 54% activity compared to the wild-type | Mus musculus |
| 3.4.22.34 | S195A | site-directed mutagenesis, control mutant, as active as the wild-type | Mus musculus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.22.34 | lysosome | - |
Mus musculus | 5764 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.22.34 | 35000 | - |
x * 35000, wild-type and mutants enzymes, SDS-PAGE | Mus musculus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.22.34 | protein + H2O | Mus musculus | - |
peptides | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.22.34 | Mus musculus | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.22.34 | benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O | - |
Mus musculus | benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.22.34 | protein + H2O | - |
Mus musculus | peptides | - |
? | |
| 3.4.22.34 | protein + H2O | substrate specificity is dominated by the interaction of the S1 subsite | Mus musculus | peptides | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.22.34 | ? | x * 35000, wild-type and mutants enzymes, SDS-PAGE | Mus musculus |
| 3.4.22.34 | More | comparison of the tertiary structure of the enzyme with other cysteine endopeptidases | Mus musculus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.22.34 | aspartate-specific endopeptidase | - |
Mus musculus |
| 3.4.22.34 | lysosomal asparaginycysteine endopeptidase | - |
Mus musculus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.22.34 | 25 | - |
assay at | Mus musculus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.22.34 | 5.8 | - |
assay at | Mus musculus |
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