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Literature summary for 3.5.1.52 extracted from

  • Gosain, A.; Lohia, R.; Shrivastava, A.; Saran, S.
    Identification and characterization of peptide: N-glycanase from Dictyostelium discoideum (2012), BMC Biochem., 13, 9-20.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.52

Cloned(Commentary)

Cloned (Comment) Organism
gene Ddpngase, single copy gene, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression under control of the constitutive promoter actin 15 and fused to enhanced yellow fluorescent protein (EYFP), in the mutant axenic strain Ax2 Dictyostelium discoideum

Protein Variants

Protein Variants Comment Organism
additional information generation of a Ddpngase gene disruption construct, a png-/Ax2 knockout strain, knockout mutants show defect in aggregation Dictyostelium discoideum

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol the recombinant fluorescent-tagged enzyme is also present to a lower extent in the cytosol Dictyostelium discoideum 5829
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additional information localized in close proximity to the proteasomal machinery Dictyostelium discoideum
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nucleus the recombinant fluorescent-tagged enzyme colocalizes in the nucleus along with DAPI blue stained DNA Dictyostelium discoideum 5634
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Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ enzyme-bound via the CXXC motif Dictyostelium discoideum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Dictyostelium discoideum the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity ?
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 ?
additional information Dictyostelium discoideum NC-4 / ATCC 24697 the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity ?
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 ?

Organism

Organism UniProt Comment Textmining
Dictyostelium discoideum Q55FC8 gene Ddpngase
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Dictyostelium discoideum NC-4 / ATCC 24697 Q55FC8 gene Ddpngase
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Source Tissue

Source Tissue Comment Organism Textmining
additional information expression levels and patterns of Ddpngase are developmentally regulated. Higher level of enzyme expression during the aggregate stage. The expression gets restricted to the prestalk region during later developmental stages Dictyostelium discoideum
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity Dictyostelium discoideum ?
-
 ?
additional information the enzyme catalyzes a deglycosylation reaction and cleaves at beta-aspartyl glucosylamine bond and removes complete glycan moiety from the glycoprotein substrate. Its reaction is different from transglutaminase catalyzed transamidating or amide bond formation reaction. The Dictyostelium discoideum PNGase is a functional peptide:N-glycanase enzyme possessing deglycosylation activity, but does not possess any significant transamidation activity Dictyostelium discoideum NC-4 / ATCC 24697 ?
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 ?

Subunits

Subunits Comment Organism
More domain organization and tertiary structure modeling, overview Dictyostelium discoideum

Synonyms

Synonyms Comment Organism
peptide: N-glycanase
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 Dictyostelium discoideum
PNGase
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 Dictyostelium discoideum

General Information

General Information Comment Organism
evolution the enzyme from Dictyostelium discoideum is a member of transglutaminase (TG) -like superfamily and shows presence of a common transglutaminase core domain and sequence homology with the known PNGases, the tertiary structure matches with the mouse PNGase. DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252, corresponding to the conserved core residues of other PNGases. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis Dictyostelium discoideum
malfunction an enzyme knockout results in small sized aggregates, all of which do not form fruiting bodies. Knockout mutants show defect in aggregation, penotypes, overview Dictyostelium discoideum
metabolism the enzyme is proposed to participate in the proteasome dependent glycoprotein degradation pathway Dictyostelium discoideum
additional information DdPNGase possess the catalytic triad residues Cys210, His237 and Asp252. DdPNGase also possess the corresponding Trp239 and Trp248, Arg229 and Glu241 conserved residues which possibly are essential for catalysis, structure homology modeling, overview Dictyostelium discoideum
physiological function the enzyme is an essential protein, important in aggregation during multicellular development of the organism Dictyostelium discoideum