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Literature summary for 3.2.1.96 extracted from

  • Maeda, M.; Kimura, Y.
    Structural features of free N-glycans occurring in plants and functional features of de-N-glycosylation enzymes, ENGase, and PNGase: the presence of unusual plant complex type N-glycans (2014), Front. Plant Sci., 5, 429.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.96

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Arabidopsis thaliana 5829
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme hydrolyzes the glycosidic linkage in the N-acetylchitobiosyl unit to form the GN1 type free N-glycans with only one GlcNAc residue at the reducing end. The enzyme shows strong activity against high-mannose type N-glycans having Manalpha(1->2)Manalpha(1->3)Manbeta1-unit, but no activity against plant complex and truncated structures having GlcNAcbeta(1->4)(Fucalpha(1->3))GlcNAc-unit at their reducing ends Arabidopsis thaliana ?
-
 ?

Subunits

Subunits Comment Organism
? x * about 70000, SDS-PAGE Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
endo-beta-N-acetylglucosaminidase
-
 Arabidopsis thaliana
ENGase
-
 Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 around pH 6.5 Arabidopsis thaliana

General Information

General Information Comment Organism
metabolism the enzyme is involved in the degradation mechanism of misfolded glycoproteins carrying exclusively high-mannose type N-glycans in the cytosol Arabidopsis thaliana