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Literature summary for 3.2.1.52 extracted from

  • Kim, Y.K.; Kim, K.R.; Kang, D.G.; Jang, S.Y.; Kim, Y.H.; Cha, H.J.
    Suppression of beta-N-acetylglucosaminidase in the N-glycosylation pathway for complex glycoprotein formation in Drosophila S2 cells (2009), Glycobiology, 19, 301-308.
    View publication on PubMed
Search for more literature for 3.2.1.52

Application

Application Comment Organism
medicine GlcNAcase may be an important factor in the formation of paucimannosidic core N-glycans in Drosophila S2 cells. It may be possible to express complex glycoproteins in engineered Drosophila S2 cells by suppressing GlcNAcase in the N-glycosylation pathway Drosophila melanogaster

Inhibitors

Inhibitors Comment Organism Structure
2-acetamido-1,2-dideoxynojirimycin GlcNAcase suppression improves the N-glycan patterns in S2 cells Drosophila melanogaster
RNAi mediates mRNA suppression in S2 cells. About 50% reduction of Glc-NAcase activity through RNAi-mediated suppression regardless of applied dsRNA amounts compared to the case of original human erythropoietin-expressing S2 cells. GlcNAcase suppression decreases the amount of terminal Man available Drosophila melanogaster

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Drosophila melanogaster 16020
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Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
S2 cell transfected with human erythropoietin Drosophila melanogaster
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-N-acetyl-D-glucosaminide + H2O
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 Drosophila melanogaster 4-nitrophenol + N-acetyl-beta-D-glucosamine
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 ?

Synonyms

Synonyms Comment Organism
beta-N-acetylglucosaminidase
-
 Drosophila melanogaster
GlcNAcase
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 Drosophila melanogaster