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Literature summary for 3.5.1.26 extracted from

  • Vinchon, S.; Moreau, S.J.; Drezen, J.M.; Prevost, G.; Cherqui, A.
    Molecular and biochemical analysis of an aspartylglucosaminidase from the venom of the parasitoid wasp Asobara tabida (Hymenoptera: Braconidae) (2010), Insect Biochem. Mol. Biol., 40, 38-48.
    View publication on PubMed
Search for more literature for 3.5.1.26

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
 Asobara tabida 5764
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
16500
-
 2 * 20700 + 2 * 16500, calculated from amino acid sequence Asobara tabida
18000
-
 2 * 30000 + 2 * 18000, active enzyme, SDS-PAGE Asobara tabida
20700
-
 2 * 20700 + 2 * 16500, calculated from amino acid sequence Asobara tabida
30000
-
 2 * 30000 + 2 * 18000, active enzyme, SDS-PAGE Asobara tabida
36740
-
 deduced polypeptide with the signal peptide cleaved off, calculated from amino acid sequence Asobara tabida
44000
-
 2 * 44000, precursor, SDS-PAGE Asobara tabida
84000
-
 precursor, SDS-PAGE Asobara tabida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Asobara tabida AGA hydrolyzes the beta-N glycosidic linkage between the asparagines residue and the N-acetylglucosamine moiety. The enzyme fails to exhibit any glycopeptide N-glycosidase activity toward entire glycoproteins like fetuin, its activity is restricted to the deglycosylation of free glycosylasparagines like human aspartylglucosaminidase ?
-
 ?

Organism

Organism UniProt Comment Textmining
Asobara tabida D0V0N4
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein two potential N-glycosylation sites are detected along the sequence at Asn52 and Asn153 Asobara tabida

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Asobara tabida
-
venom gland
-
 Asobara tabida
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information AGA hydrolyzes the beta-N glycosidic linkage between the asparagines residue and the N-acetylglucosamine moiety. The enzyme fails to exhibit any glycopeptide N-glycosidase activity toward entire glycoproteins like fetuin, its activity is restricted to the deglycosylation of free glycosylasparagines like human aspartylglucosaminidase Asobara tabida ?
-
 ?
N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O
-
 Asobara tabida N-acetyl-D-glucosaminylamine + L-aspartate
-
 ?

Subunits

Subunits Comment Organism
heterotetramer 2 * 20700 + 2 * 16500, calculated from amino acid sequence Asobara tabida
heterotetramer 2 * 30000 + 2 * 18000, active enzyme, SDS-PAGE Asobara tabida
homodimer 2 * 44000, precursor, SDS-PAGE Asobara tabida

Synonyms

Synonyms Comment Organism
AGA
-
 Asobara tabida
aspartylglucosaminidase
-
 Asobara tabida
glycosylasparaginase
-
 Asobara tabida

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Asobara tabida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Asobara tabida