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Literature summary for 3.5.1.26 extracted from
- Biochemical characterization and comparison of aspartylglucosaminidases secreted in venom of the parasitoid wasps Asobara tabida and Leptopilina heterotoma (2017), PLoS ONE, 12, e0181940 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene AGA, DNA and amino acid sequence determination and analysis, sequence comparisons with human enzyme and Asobara tabida enzyme | Leptopilina heterotoma |
| gene AGA, DNA and amino acid sequence determination and analysis, sequence comparisons with human enzyme and Leptopilina heterotoma enzyme | Asobara tabida |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| L-asparagine | competitively inhibits the hydrolysis of aspartylglucosamine, 40-45% inhibition at 2 mM | Asobara tabida |  |
| L-asparagine | competitively inhibits the hydrolysis of aspartylglucosamine, 40-45% inhibition at 2 mM | Leptopilina heterotoma | |
| additional information | no inhibiton by 5 mM L-glutamine | Asobara tabida | |
| additional information | no inhibiton ba 5 mM L-glutamine | Leptopilina heterotoma |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics | Asobara tabida | |
| additional information | - |
additional information | kinetics | Leptopilina heterotoma | |
| 0.0449 | - |
L-aspartyl-beta-(7-amido-4-methylcoumarin) | pH 8.0, temperature not specified in the publication, recombinant enzyme | Leptopilina heterotoma | |
| 0.0742 | - |
L-aspartyl-beta-(7-amido-4-methylcoumarin) | pH 8.0, temperature not specified in the publication, recombinant enzyme | Asobara tabida | |
| 1.188 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, recombinant enzyme | Leptopilina heterotoma | |
| 4.051 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, recombinant enzyme | Asobara tabida | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | high amounts of AGA-like protein is secreted in the venom, the venom AGA is secreted as fully activated enzyme | Asobara tabida | - |
- |
| extracellular | high amounts of AGA-like protein is secreted in the venom, the venom AGA is secreted as fully activated enzyme | Leptopilina heterotoma | - |
- |
| additional information | the enzyme has a signal peptide | Asobara tabida | - |
- |
| additional information | the enzyme has a signal peptide | Leptopilina heterotoma | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Asobara tabida | D0V0N4 | from populations collected in Sainte-Foy-les-Lyon (France) | - |
| Leptopilina heterotoma | A0A141NXG8 | from populations collected in Gotheron (France) | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | only the alpha AGA subunits are glycosylated, and these glycosylations are partially resistant to PGNase F treatment, N-glycosylation sites prediction, overview | Asobara tabida |
| glycoprotein | only the beta AGA subunits are glycosylated, and these glycosylations are partially resistant to PGNase F treatment, N-glycosylation sites prediction, overview | Leptopilina heterotoma |
| proteolytic modification | the enzyme is precessed through autocatalytic cleavage, extracellular autocleavage and autoactivation | Leptopilina heterotoma |
| proteolytic modification | the enzyme is processed through autocatalytic cleavage, extracellular autocleavage and autoactivation | Asobara tabida |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | the wasps are reared at 25°C on a susceptible Drosophila melanogaster strain (Gif stock 1333) | Asobara tabida | - |
| additional information | the wasps are reared at 25°C on a susceptible Drosophila melanogaster strain (Gif stock 1333) | Leptopilina heterotoma | - |
| venom | - |
Asobara tabida | - |
| venom | - |
Leptopilina heterotoma | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-asparagine + H2O | - |
Asobara tabida | L-aspartate + NH3 | - |
ir | |
| L-asparagine + H2O | - |
Leptopilina heterotoma | L-aspartate + NH3 | - |
ir | |
| L-aspartyl-beta-(7-amido-4-methylcoumarin) + H2O | - |
Asobara tabida | L-aspartic acid + 7-amino-4-methylcoumarin | - |
ir | |
| L-aspartyl-beta-(7-amido-4-methylcoumarin) + H2O | - |
Leptopilina heterotoma | L-aspartic acid + 7-amino-4-methylcoumarin | - |
ir | |
| L-aspartylglucosamine + H2O | - |
Asobara tabida | L-aspartate + glucosamine | - |
ir | |
| L-aspartylglucosamine + H2O | - |
Leptopilina heterotoma | L-aspartate + glucosamine | - |
ir | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterotetramer | 2 * 21000 + 2 * 16000, about, (alphabeta)2, sequence calculation, 2 * 25000-27000 + 2 * 16000, SDS-PAGE | Asobara tabida |
| heterotetramer | 2 * 21000 + 2 * 17000, about, (alphabeta)2, sequence calculation, 2 * 21000 + 2 * 20000, SDS-PAGE | Leptopilina heterotoma |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AGA | - |
Asobara tabida |
| AGA | - |
Leptopilina heterotoma |
| aspartylglucosaminidase | - |
Asobara tabida |
| aspartylglucosaminidase | - |
Leptopilina heterotoma |
| AtAGA | - |
Asobara tabida |
| LhAGA | - |
Leptopilina heterotoma |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Asobara tabida |
| 8 | - |
- |
Leptopilina heterotoma |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 8 | high activity at | Asobara tabida |
| 6 | 8 | high activity at | Leptopilina heterotoma |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the venom AGAs have a similar domain organization as mammalian AGAs. They share key residues for autocatalysis and activity, and the mature alpha- and beta-subunits also form an (alphabeta)2 structure in solution. Only one of the AGAs subunits, the beta for LhAGA, is glycosylated instead of the two subunits for lysosomal human AGA (hAGA) | Leptopilina heterotoma |
| evolution | the venom AGAs have a similar domain organization as mammalian AGAs. They share with them key residues for autocatalysis and activity, and the mature alpha- and beta-subunits also form an (alphabeta)2 structure in solution. Only one of the AGAs subunits (alpha for AtAGA) is glycosylated instead of the two subunits for lysosomal human AGA (hAGA) | Asobara tabida |
| additional information | residue T206 is essential for enzyme catalysis and autocatalytic activation, and the W34, R234 and D237 residues, involved in substrate binding, are conserved. Homology structure modeling, structure comparisons, overview | Leptopilina heterotoma |
| additional information | residues T206 residue, essential for enzyme catalysis and autocatalytic activation, and the W34, R234 and D237 residues, involved in substrate binding, are conserved. Homology structure modeling, structure comparisons, overview | Asobara tabida |
| physiological function | once AGAs are injected into the larvae of the Drosophila melanogaster host, the asparaginase activity may play a role in modulating their physiology | Asobara tabida |
| physiological function | once AGAs are injected into the larvae of the Drosophila melanogaster host, the asparaginase activity may play a role in modulating their physiology | Leptopilina heterotoma |
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