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Literature summary extracted from

  • Coulette, Q.; Lemauf, S.; Colinet, D.; Prevost, G.; Anselme, C.; Poirie, M.; Gatti, J.L.
    Biochemical characterization and comparison of aspartylglucosaminidases secreted in venom of the parasitoid wasps Asobara tabida and Leptopilina heterotoma (2017), PLoS ONE, 12, e0181940 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.26 gene AGA, DNA and amino acid sequence determination and analysis, sequence comparisons with human enzyme and Asobara tabida enzyme Leptopilina heterotoma
3.5.1.26 gene AGA, DNA and amino acid sequence determination and analysis, sequence comparisons with human enzyme and Leptopilina heterotoma enzyme Asobara tabida

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.26 L-asparagine competitively inhibits the hydrolysis of aspartylglucosamine, 40-45% inhibition at 2 mM Asobara tabida
3.5.1.26 L-asparagine competitively inhibits the hydrolysis of aspartylglucosamine, 40-45% inhibition at 2 mM Leptopilina heterotoma
3.5.1.26 additional information no inhibiton by 5 mM L-glutamine Asobara tabida
3.5.1.26 additional information no inhibiton ba 5 mM L-glutamine Leptopilina heterotoma

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.26 additional information
-
 additional information kinetics Asobara tabida
3.5.1.26 additional information
-
 additional information kinetics Leptopilina heterotoma
3.5.1.26 0.0449
-
 L-aspartyl-beta-(7-amido-4-methylcoumarin) pH 8.0, temperature not specified in the publication, recombinant enzyme Leptopilina heterotoma
3.5.1.26 0.0742
-
 L-aspartyl-beta-(7-amido-4-methylcoumarin) pH 8.0, temperature not specified in the publication, recombinant enzyme Asobara tabida
3.5.1.26 1.188
-
 L-asparagine pH 8.0, temperature not specified in the publication, recombinant enzyme Leptopilina heterotoma
3.5.1.26 4.051
-
 L-asparagine pH 8.0, temperature not specified in the publication, recombinant enzyme Asobara tabida

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.26 extracellular high amounts of AGA-like protein is secreted in the venom, the venom AGA is secreted as fully activated enzyme Asobara tabida
-
-
3.5.1.26 extracellular high amounts of AGA-like protein is secreted in the venom, the venom AGA is secreted as fully activated enzyme Leptopilina heterotoma
-
-
3.5.1.26 additional information the enzyme has a signal peptide Asobara tabida
-
-
3.5.1.26 additional information the enzyme has a signal peptide Leptopilina heterotoma
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.26 Asobara tabida D0V0N4 from populations collected in Sainte-Foy-les-Lyon (France)
-
3.5.1.26 Leptopilina heterotoma A0A141NXG8 from populations collected in Gotheron (France)
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.1.26 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
3.5.1.26 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
3.5.1.26 proteolytic modification the enzyme is precessed through autocatalytic cleavage, extracellular autocleavage and autoactivation Leptopilina heterotoma
3.5.1.26 proteolytic modification the enzyme is processed through autocatalytic cleavage, extracellular autocleavage and autoactivation Asobara tabida

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.26 additional information the wasps are reared at 25°C on a susceptible Drosophila melanogaster strain (Gif stock 1333) Asobara tabida
-
3.5.1.26 additional information the wasps are reared at 25°C on a susceptible Drosophila melanogaster strain (Gif stock 1333) Leptopilina heterotoma
-
3.5.1.26 venom
-
 Asobara tabida
-
3.5.1.26 venom
-
 Leptopilina heterotoma
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.26 L-asparagine + H2O
-
 Asobara tabida L-aspartate + NH3
-
 ir
3.5.1.26 L-asparagine + H2O
-
 Leptopilina heterotoma L-aspartate + NH3
-
 ir
3.5.1.26 L-aspartyl-beta-(7-amido-4-methylcoumarin) + H2O
-
 Asobara tabida L-aspartic acid + 7-amino-4-methylcoumarin
-
 ir
3.5.1.26 L-aspartyl-beta-(7-amido-4-methylcoumarin) + H2O
-
 Leptopilina heterotoma L-aspartic acid + 7-amino-4-methylcoumarin
-
 ir
3.5.1.26 L-aspartylglucosamine + H2O
-
 Asobara tabida L-aspartate + glucosamine
-
 ir
3.5.1.26 L-aspartylglucosamine + H2O
-
 Leptopilina heterotoma L-aspartate + glucosamine
-
 ir

Subunits

EC Number Subunits Comment Organism
3.5.1.26 heterotetramer 2 * 21000 + 2 * 16000, about, (alphabeta)2, sequence calculation, 2 * 25000-27000 + 2 * 16000, SDS-PAGE Asobara tabida
3.5.1.26 heterotetramer 2 * 21000 + 2 * 17000, about, (alphabeta)2, sequence calculation, 2 * 21000 + 2 * 20000, SDS-PAGE Leptopilina heterotoma

Synonyms

EC Number Synonyms Comment Organism
3.5.1.26 AGA
-
 Asobara tabida
3.5.1.26 AGA
-
 Leptopilina heterotoma
3.5.1.26 aspartylglucosaminidase
-
 Asobara tabida
3.5.1.26 aspartylglucosaminidase
-
 Leptopilina heterotoma
3.5.1.26 AtAGA
-
 Asobara tabida
3.5.1.26 LhAGA
-
 Leptopilina heterotoma

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.26 8
-
-
 Asobara tabida
3.5.1.26 8
-
-
 Leptopilina heterotoma

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.26 6 8 high activity at Asobara tabida
3.5.1.26 6 8 high activity at Leptopilina heterotoma

General Information

EC Number General Information Comment Organism
3.5.1.26 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
3.5.1.26 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
3.5.1.26 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
3.5.1.26 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
3.5.1.26 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
3.5.1.26 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