Application | Comment | Organism |
---|---|---|
analysis | the facile expression, non-glycosylated nature, unusual pH optimum and broad substrate specificity of the enzyme makes recombinant PNGase H+ a versatile tool in N-glycan analysis | Terriglobus roseus |
Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis, recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3) | Terriglobus roseus |
General Stability | Organism |
---|---|
the recombinantly expressed enzyme is rapidly degraded after Escherichia coli cell lysis in Tris/HCl buffer which is commonly used in cell disruption procedures, although a protease inhibitor is added | Terriglobus roseus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-mercaptoethanol | 20% inhibition at 100 mM | Terriglobus roseus | |
Triton X100 | 40% inhibition at 1% | Terriglobus roseus | |
Urea | 80% inhibition at 2 M | Terriglobus roseus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | no metal ion requirements | Terriglobus roseus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
70000 | - |
x * 70000, recombinant enzyme, SDS-PAGE, x 61500, about, sequence calculation | Terriglobus roseus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Terriglobus roseus | - |
- |
- |
Terriglobus roseus DSM 18391 | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
no glycoprotein | - |
Terriglobus roseus |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinit chromatography | Terriglobus roseus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dabcyl-Gly-Glu-Asn-(GlcNAcbeta(1->2)Manalpha(1->3)[GlcNAcbeta(1->2)Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta)-Arg + H2O | - |
Terriglobus roseus | GlcNAcbeta(1->2)Manalpha(1->3)[GlcNAcbeta(1->2)Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + dabcyl-Gly-Glu-Asn-Arg | - |
? | |
dabcyl-Gly-Glu-Asn-(GlcNAcbeta(1->2)Manalpha(1->3)[GlcNAcbeta(1->2)Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta)-Arg + H2O | - |
Terriglobus roseus DSM 18391 | GlcNAcbeta(1->2)Manalpha(1->3)[GlcNAcbeta(1->2)Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc + dabcyl-Gly-Glu-Asn-Arg | - |
? | |
additional information | heat-denatured RNase B and lactoferrin are almost completely deglycosylated by PNGaseH+, profiles of N-glycan products released from the substrates, similar to PNGase F, overview. The acidic enzyme, termed PNGase H+, shows an extremely low pH optimum with a broad substrate specificity. The recombinant PNGase H+ can liberate high mannose-, hybrid- and complex-type N-glycans including core alpha1,3-fucosylated oligosaccharides from both glycoproteins and glycopeptides. PNGase H+ exhibits a better release efficiency over N-glycans without core alpha1,3-fucose compared with PNGase A | Terriglobus roseus | ? | - |
? | |
additional information | heat-denatured RNase B and lactoferrin are almost completely deglycosylated by PNGaseH+, profiles of N-glycan products released from the substrates, similar to PNGase F, overview. The acidic enzyme, termed PNGase H+, shows an extremely low pH optimum with a broad substrate specificity. The recombinant PNGase H+ can liberate high mannose-, hybrid- and complex-type N-glycans including core alpha1,3-fucosylated oligosaccharides from both glycoproteins and glycopeptides. PNGase H+ exhibits a better release efficiency over N-glycans without core alpha1,3-fucose compared with PNGase A | Terriglobus roseus DSM 18391 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 70000, recombinant enzyme, SDS-PAGE, x 61500, about, sequence calculation | Terriglobus roseus |
Synonyms | Comment | Organism |
---|---|---|
N-glycanase | - |
Terriglobus roseus |
peptide N-glycosidase | - |
Terriglobus roseus |
peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase | - |
Terriglobus roseus |
PNGase H+ | - |
Terriglobus roseus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Terriglobus roseus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
2.6 | - |
- |
Terriglobus roseus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
2 | 3.5 | remarkable loss of activity above pH 3.5, narrow pH range, profile overview | Terriglobus roseus |