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3.5.1.52: peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase

This is an abbreviated version!
For detailed information about peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase, go to the full flat file.

Word Map on EC 3.5.1.52

Reaction

Manalpha(1-6)(Xylbeta(1-2))Manbeta(1-4)GlcNAcbeta(1-4)(Fucalpha(1-3))GlcNAc-Asn-Asp-Glu-Ser-Ser
+
H2O
=
Manalpha(1-6)(Xylbeta(1-2))Manbeta(1-4)GlcNAcbeta(1-4)(Fucalpha(1-3))GlcNAc
 +
Asn-Asp-Glu-Ser-Ser

Synonyms

acid PNGase M, acidic peptide:N-glycanase, acidic PNGase, aPNGase, At3g14920, At5g05480, AtPNG1, DDB0189828, EC 3.2.2.18, glycoamidase, glycopeptidase, glycopeptide N-glycosidase, jackbean glycopeptidase, L-929 PNGase, MPng1, N-glycanase, N-glycosidase F, N-oligosaccharide glycopeptidase, Ncpng1, neutral PNGase M, Ngly1, peptide N-glycanase, peptide N-glycosidase, peptide N-glycosidase F, peptide N4(N-acetyl-glucosaminyl)asparagine amidase, peptide-N-(N-acetyl-beta-glucosaminyl) asparagine amidase F, peptide-N-glycanase, peptide-N-glycosidase F, peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F, peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase, peptide: N-glycanase, peptide: N-glycosidase, peptide:N-glycanase, peptide:N-glycanase homolog, peptide:N-glycosidase, peptidyl N-glycanase F, PGNase, PNG-1, PNG1, Png1p, PNGase, PNGase A, PNGase A-like enzyme, PNGase At, PNGase F, PNGase F-II, PNGase H+, PNGase J, PNGase Os, PNGase Se, PNGase Yl, PNGase-A, PNGaseF, Pngl, SpPNGase, TGc domain-containing protein, yeast peptide: N-glycanase, YPng, YPng1

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.52 peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase

Crystallization

Crystallization on EC 3.5.1.52 - peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
purified wild-type PUB domain, also as selenomethionine variants, by sitting drop vapour diffusion method at 17°C, with a reservoir solution containing 0.2 M sodium acetate, 0.1 M Tris, pH 8.5, 30% PEG 4000, using 20% glycerol as cryoprotectant, X-ray diffraction structure determination and analysis at 1.6 A resolution, mutant L66M/L75M/L87M PUB domain are crystallized in 50% PEG 400, 0.1 M CHES, pH 9.5, 0.2 M NaCl, molecular replacement, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
hanging drop vapor diffusion, crystal structure of the N-terminal domain of PNGase in complex with the cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus provides detailed insight into the interaction between p97 and its substrate-processing cofactors
purified recombinant enzyme core domain and XPCB domain in complex with the recombinant murine HR23B protein, 9.5 mg/ml of enzyme domains in a 1:1 ratio, vapour diffusion method, against reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 28-32% PEG 4000, 0.2 M sodium acetate, heavy atom derivatization by soaking in 1 mM ethyl mercury thiosalicylate, 1 mM K2[PtCN4], or 1 mM KAuCN2 for 4 h, cryoprotection by 20% glycerol, X-ray diffraction structure determination and analysis at 1.85 A resolution
-
the crystal structure of PNGase in complex with N,N'-diacetylchitobiose is described, refined at 3.4 A