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 | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | - |
Yarrowia lipolytica | |
Fe3+ | - |
Yarrowia lipolytica | |
Mn2+ | - |
Yarrowia lipolytica | |
Zn2+ | - |
Yarrowia lipolytica |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | no metal ions are required for full activity | Yarrowia lipolytica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Yarrowia lipolytica | - |
- |
- |
Yarrowia lipolytica SMS397A | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme PNGase Yl from Pichia pastoris strain GS115 by ultracentrifugatio, dialysis, and nickel affinity chromatography | Yarrowia lipolytica |
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 | Comment | Organism |
---|---|---|
acidic peptide:N-glycanase | - |
Yarrowia lipolytica |
PNGase A-like enzyme | - |
Yarrowia lipolytica |
PNGase Yl | - |
Yarrowia lipolytica |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
recombinant enzyme | Yarrowia lipolytica |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
recombinant enzyme | Yarrowia lipolytica |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
3 | 7.5 | activity range, profile overview | Yarrowia lipolytica |
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 |