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Literature summary for 3.5.1.52 extracted from

  • Wang, T.; Cai, Z.P.; Gu, X.Q.; Ma, H.Y.; Du, Y.M.; Huang, K.; Voglmeir, J.; Liu, L.
    Discovery and characterization of a novel extremely acidic bacterial N-glycanase with combined advantages of PNGase F and A (2014), Biosci. Rep., 34, e00149.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.52

Application

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(Commentary)

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

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

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

Metals/Ions Comment Organism Structure
additional information no metal ion requirements Terriglobus roseus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
 x * 70000, recombinant enzyme, SDS-PAGE, x 61500, about, sequence calculation Terriglobus roseus

Organism

Organism UniProt Comment Textmining
Terriglobus roseus
-
-
-
Terriglobus roseus DSM 18391
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no glycoprotein
-
 Terriglobus roseus

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinit chromatography Terriglobus roseus

Substrates and Products (Substrate)

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

Subunits Comment Organism
? x * 70000, recombinant enzyme, SDS-PAGE, x 61500, about, sequence calculation Terriglobus roseus

Synonyms

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Terriglobus roseus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6
-
-
 Terriglobus roseus

pH Range

pH Minimum pH Maximum Comment Organism
2 3.5 remarkable loss of activity above pH 3.5, narrow pH range, profile overview Terriglobus roseus