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Literature summary for 3.4.22.34 extracted from
- Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis (2007), Insect Biochem. Mol. Biol., 37, 911-922.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| plasmid pTrcHisB/HlLgm transformed into the Escherichia coli Top10F0 strain | Haemaphysalis longicornis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| egg white cystatin | concentration of 2 microM, 45.13% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
| iodoacetamide | concentration of 3 mM, 100% inhibition of recombinant protein activity, BSA cleavage inhibited by 5 mM iodoacetamide | Haemaphysalis longicornis |  |
| leupeptin | concentration of 300 microM, 16.07% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
| N-ethylmaleimide | concentration of 3 mM, 95.74% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
| pepstatin | concentration of 500 microM, 7.8% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
| phenylmethanesulfonyl fluoride | PMSF, concentration of 5 mM, 19% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
| trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane | E-64, concentration of 500 microM, 8.88% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | bound | Haemaphysalis longicornis | 16020 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 38000 | - |
removal of a peptide of 9000 Dalton from the preprotein | Haemaphysalis longicornis |
| 47000 | - |
preprotein, deduced from sequence | Haemaphysalis longicornis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haemaphysalis longicornis | A4PF00 | encoded by the HlLgm gene; parthenogenetic Okayama strain | - |
| Haemaphysalis longicornis Okayama | A4PF00 | encoded by the HlLgm gene; parthenogenetic Okayama strain | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | cleavage site at asparagines 364-365 at the C-terminus identified in endogenous and in recombinant protein | Haemaphysalis longicornis |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| SDS-PAGE | Haemaphysalis longicornis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| midgut | lmidgut epithelium shown by immunohistochemistry | Haemaphysalis longicornis | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.642 | - |
recombinant protein, 37°C, pH 7, benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide, activity profile shown, inhibition assay described, up-regulation by the host blood-feeding process shown by in vitro proteolysis assay | Haemaphysalis longicornis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O | recombinant protein | Haemaphysalis longicornis | benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin | - |
? | |
| benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O | recombinant protein | Haemaphysalis longicornis Okayama | benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin | - |
? | |
| Bovine serum albumin + H2O | degradation in a dose-dependent manner at pH 7 and 30°C during 6 h of incubation, no cleavage detected at or above 37°C, strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines shown | Haemaphysalis longicornis | ? | - |
? | |
| Bovine serum albumin + H2O | degradation in a dose-dependent manner at pH 7 and 30°C during 6 h of incubation, no cleavage detected at or above 37°C, strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines shown | Haemaphysalis longicornis Okayama | ? | - |
? | |
| Hemoglobin + H2O | strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines indicated | Haemaphysalis longicornis | ? | - |
? | |
| Hemoglobin + H2O | strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines indicated | Haemaphysalis longicornis Okayama | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Asparaginyl endopeptidase | - |
Haemaphysalis longicornis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
activity assay at | Haemaphysalis longicornis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 70 | assay under different temperature conditions tested | Haemaphysalis longicornis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
activity assay at | Haemaphysalis longicornis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 11 | assay under different pH conditions tested | Haemaphysalis longicornis |
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