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Literature summary for 3.5.1.52 extracted from

  • Lee, K.J.; Gil, J.Y.; Kim, S.Y.; Kwon, O.; Ko, K.; Kim, D.I.; Kim, D.K.; Kim, H.H.; Oh, D.B.
    Molecular characterization of acidic peptide:N-glycanase from the dimorphic yeast Yarrowia lipolytica (2015), J. Biochem., 157, 35-43.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
PNGase Yl, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Pichia pastoris strain GS115 Yarrowia lipolytica

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Yarrowia lipolytica
Fe3+
-
Yarrowia lipolytica
Mn2+
-
Yarrowia lipolytica
Zn2+
-
Yarrowia lipolytica

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no metal ions are required for full activity Yarrowia lipolytica

Organism

Organism UniProt Comment Textmining
Yarrowia lipolytica
-
-
-
Yarrowia lipolytica SMS397A
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme PNGase Yl from Pichia pastoris strain GS115 by ultracentrifugatio, dialysis, and nickel affinity chromatography Yarrowia lipolytica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information using glycopeptide substrates, PNGase Yl releases various types of N-glycans including high-mannose and complex-type glycans as well as glycans containing core-linked alpha(1,3)-fucose that are frequently found in plants and insects. In comparison with PNGase A, PNGase Yl is able to cleave with higher efficiency the glycans from some denatured glycoproteins. PNGase Yl shows the highest activity toward HRP glycopeptides attached with trimannosyl core glycans containing beta(1,2)-xylose and core-linked alpha, substrate specificity, overview(1,3)-fucose Yarrowia lipolytica ?
-
?
additional information using glycopeptide substrates, PNGase Yl releases various types of N-glycans including high-mannose and complex-type glycans as well as glycans containing core-linked alpha(1,3)-fucose that are frequently found in plants and insects. In comparison with PNGase A, PNGase Yl is able to cleave with higher efficiency the glycans from some denatured glycoproteins. PNGase Yl shows the highest activity toward HRP glycopeptides attached with trimannosyl core glycans containing beta(1,2)-xylose and core-linked alpha, substrate specificity, overview(1,3)-fucose Yarrowia lipolytica SMS397A ?
-
?

Synonyms

Synonyms Comment Organism
acidic peptide:N-glycanase
-
Yarrowia lipolytica
PNGase A-like enzyme
-
Yarrowia lipolytica
PNGase Yl
-
Yarrowia lipolytica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
recombinant enzyme Yarrowia lipolytica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
recombinant enzyme Yarrowia lipolytica

pH Range

pH Minimum pH Maximum Comment Organism
3 7.5 activity range, profile overview Yarrowia lipolytica

General Information

General Information Comment Organism
evolution phylogenetic analysis of acidic PNGases, yeast PNGases are diverse and distantly related from filamentous fungi PNGases in the phylogenetic tree Yarrowia lipolytica