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Literature summary extracted from

  • Funakoshi, Y.; Negishi, Y.; Gergen, J.P.; Seino, J.; Ishii, K.; Lennarz, W.J.; Matsuo, I.; Ito, Y.; Taniguchi, N.; Suzuki, T.
    Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogaster (2010), PLoS ONE, 5, e10545.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.52 expressed in Sf21 insect cells Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.52 C165T inactive Saccharomyces cerevisiae
3.5.1.52 C165T/N166V/R167C inactive Saccharomyces cerevisiae
3.5.1.52 C191A inactive Saccharomyces cerevisiae
3.5.1.52 N166V/R167C the mutant shows 79% of wild type activity Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.52 cytosol
-
 Drosophila melanogaster 5829
-
3.5.1.52 cytosol
-
 Saccharomyces cerevisiae 5829
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.52 74000
-
 x * 74000, SDS-PAGE Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.52 Drosophila melanogaster
-
-
-
3.5.1.52 Saccharomyces cerevisiae
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.52 larva
-
 Drosophila melanogaster
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.52 additional information the Drosophila ortholog of PNGase (PngI) does not possess deglycosylation activity but retains carbohydrate-binding activity. The transglutaminase domain of Pngl participates in some type of catalytic activity even though the protein does not have the conventional deglycosylation activity Drosophila melanogaster ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.52 ? x * 74000, SDS-PAGE Drosophila melanogaster

Synonyms

EC Number Synonyms Comment Organism
3.5.1.52 peptide:N-glycanase
-
 Drosophila melanogaster
3.5.1.52 peptide:N-glycanase
-
 Saccharomyces cerevisiae
3.5.1.52 PNG1
-
 Saccharomyces cerevisiae
3.5.1.52 PNGase
-
 Drosophila melanogaster
3.5.1.52 PNGase
-
 Saccharomyces cerevisiae
3.5.1.52 Pngl
-
 Drosophila melanogaster

General Information

EC Number General Information Comment Organism
3.5.1.52 malfunction homozygous deletion mutants show developmental defect Drosophila melanogaster
3.5.1.52 physiological function the enzyme plays a critical role during larval development and metamorphosis Drosophila melanogaster