Literature summary for 3.5.1.52 extracted from

Sun, G.; Yu, X.; Bao, C.; Wang, L.; Li, M.; Gan, J.; Qu, D.; Ma, J.; Chen, L.
Identification and characterization of a novel prokaryotic peptide N-glycosidase from Elizabethkingia meningoseptica (2015), J. Biol. Chem., 290, 7452-7462 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene PNGase F-II, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of His6-tagged wild-type and selenomethionine-labeled enzyme in Escherichia coli strain BL21(DE3)	Elizabethkingia meningoseptica

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified His6-tagged wild-type and selenomethionine-labeled enzymes, hanging drop vapor diffusion method, method optimization, SeMet-labeled enzyme from 10% PEG 4000, 0.01 M MgCl2, 0.2 M KCl, and 0.05 M sodium cacodylate, pH 6.5, and native PNGase F-II crystals from 12% PEG 3350 and 0.1 M sodium malonate, pH 7.0, 16°C, X-ray diffraction structure determination and analysis at 2.8 A and 1.9 A resolution, respectively, molecular replacement using the structure of native PNGase F-II as the search model	Elizabethkingia meningoseptica

Crystallization (Comment)

Organism

purified His6-tagged wild-type and selenomethionine-labeled enzymes, hanging drop vapor diffusion method, method optimization, SeMet-labeled enzyme from 10% PEG 4000, 0.01 M MgCl2, 0.2 M KCl, and 0.05 M sodium cacodylate, pH 6.5, and native PNGase F-II crystals from 12% PEG 3350 and 0.1 M sodium malonate, pH 7.0, 16°C, X-ray diffraction structure determination and analysis at 2.8 A and 1.9 A resolution, respectively, molecular replacement using the structure of native PNGase F-II as the search model

Elizabethkingia meningoseptica

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	bound at the C-terminus of the recombinant enzyme, Zn2+ is derived from the pET28a expression vector	Elizabethkingia meningoseptica

Organism

Organism	UniProt	Comment	Textmining
Elizabethkingia meningoseptica	A0A090KI56	clinical isolate FMS-007	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration	Elizabethkingia meningoseptica

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
horse radish peroxidase + H2O	only PNGase F-II can release alpha->1,3 core-fucosylated glycans from HRP	Elizabethkingia meningoseptica	?	-	?

Synonyms

Synonyms	Comment	Organism
peptide: N-glycosidase	-	Elizabethkingia meningoseptica
peptide:N-glycosidase	-	Elizabethkingia meningoseptica
PNGase	-	Elizabethkingia meningoseptica
PNGase F-II	-	Elizabethkingia meningoseptica

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Elizabethkingia meningoseptica

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Elizabethkingia meningoseptica

General Information

General Information	Comment	Organism
additional information	structural comparison with PNGase F reveals a relatively larger glycan-binding groove in the catalytic domain and an additional bowl-like domain at the N-terminus of the protein	Elizabethkingia meningoseptica
physiological function	PNGase F-II might have a function distinct from that of PNGase F	Elizabethkingia meningoseptica