Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
3.5.1.52 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

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

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.52 Yarrowia lipolytica
-
-
-
3.5.1.52 Yarrowia lipolytica SMS397A
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.52 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 ?
-
 ?
3.5.1.52 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.52 35
-
 recombinant enzyme Yarrowia lipolytica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.52 5
-
 recombinant enzyme Yarrowia lipolytica

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.52 3 7.5 activity range, profile overview Yarrowia lipolytica

General Information

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