EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.22.34 | plasmid pTrcHisB/HlLgm transformed into the Escherichia coli Top10F0 strain | Haemaphysalis longicornis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.22.34 | egg white cystatin | concentration of 2 microM, 45.13% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
3.4.22.34 | iodoacetamide | concentration of 3 mM, 100% inhibition of recombinant protein activity, BSA cleavage inhibited by 5 mM iodoacetamide | Haemaphysalis longicornis | |
3.4.22.34 | leupeptin | concentration of 300 microM, 16.07% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
3.4.22.34 | N-ethylmaleimide | concentration of 3 mM, 95.74% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
3.4.22.34 | pepstatin | concentration of 500 microM, 7.8% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
3.4.22.34 | phenylmethanesulfonyl fluoride | PMSF, concentration of 5 mM, 19% inhibition of recombinant protein activity | Haemaphysalis longicornis | |
3.4.22.34 | trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane | E-64, concentration of 500 microM, 8.88% inhibition of recombinant protein activity | Haemaphysalis longicornis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.22.34 | membrane | bound | Haemaphysalis longicornis | 16020 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.4.22.34 | 38000 | - |
removal of a peptide of 9000 Dalton from the preprotein | Haemaphysalis longicornis |
3.4.22.34 | 47000 | - |
preprotein, deduced from sequence | Haemaphysalis longicornis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.22.34 | Haemaphysalis longicornis | A4PF00 | encoded by the HlLgm gene; parthenogenetic Okayama strain | - |
3.4.22.34 | Haemaphysalis longicornis Okayama | A4PF00 | encoded by the HlLgm gene; parthenogenetic Okayama strain | - |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.4.22.34 | proteolytic modification | cleavage site at asparagines 364-365 at the C-terminus identified in endogenous and in recombinant protein | Haemaphysalis longicornis |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.4.22.34 | SDS-PAGE | Haemaphysalis longicornis |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.4.22.34 | midgut | lmidgut epithelium shown by immunohistochemistry | Haemaphysalis longicornis | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.4.22.34 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.22.34 | benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O | recombinant protein | Haemaphysalis longicornis | benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin | - |
? | |
3.4.22.34 | benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O | recombinant protein | Haemaphysalis longicornis Okayama | benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin | - |
? | |
3.4.22.34 | 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 | ? | - |
? | |
3.4.22.34 | 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 | ? | - |
? | |
3.4.22.34 | Hemoglobin + H2O | strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines indicated | Haemaphysalis longicornis | ? | - |
? | |
3.4.22.34 | Hemoglobin + H2O | strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines indicated | Haemaphysalis longicornis Okayama | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.22.34 | Asparaginyl endopeptidase | - |
Haemaphysalis longicornis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.22.34 | 37 | - |
activity assay at | Haemaphysalis longicornis |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.22.34 | 10 | 70 | assay under different temperature conditions tested | Haemaphysalis longicornis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.22.34 | 7 | - |
activity assay at | Haemaphysalis longicornis |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.4.22.34 | 3 | 11 | assay under different pH conditions tested | Haemaphysalis longicornis |