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Literature summary for 3.5.1.52 extracted from

  • Zhao, G.; Zhou, X.; Wang, L.; Li, G.; Kisker, C.; Lennarz, W.J.; Schindelin, H.
    Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways (2006), J. Biol. Chem., 281, 13751-13761.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of the full-length enzyme, enzyme core domain, and enzyme XPCB domain in Escherichia coli strain BL21(DE3) Mus musculus

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Mus musculus

General Stability

General Stability Organism
zinc binding stabilizes the enzyme conformation by stabilizing the intermediate state and promoting product release Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
carbobenzyloxy-Val-Ala-Asp i.e. Z-VAD, binds to the active site of the enzyme, binding structure, overview Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc binding domain structure involving a CXXC motif, zinc binding stabilizes the enzyme conformation by stabilizing the intermediate state and promoting product release Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus the enzyme removes N-linked oligosaccharides from misfolded glycoproteins as part of endoplasmic reticulum-associated degradation pathway involving a tight complex-formation with protein HR23, HR23 is also involved in DNA repair, co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways, overview ?
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Organism

Organism UniProt Comment Textmining
Mus musculus
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Purification (Commentary)

Purification (Comment) Organism
recombinant full-length enzyme, enzyme core domain, and enzyme XPCB domain from Escherichia coli strain BL21(DE3),the XPCB domain by chitin affinity chromatographyand gel filtration Mus musculus

Reaction

Reaction Comment Organism Reaction ID
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 active site structure and catalytic mechanism Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme removes N-linked oligosaccharides from misfolded glycoproteins as part of endoplasmic reticulum-associated degradation pathway involving a tight complex-formation with protein HR23, HR23 is also involved in DNA repair, co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways, overview Mus musculus ?
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?

Subunits

Subunits Comment Organism
More enzyme domain structure and enzyme-HR23 complex structure analysis, the enzyme contains a catalytic transglutaminase-like fold, a catalytic cleft structure, a zinc binding domain, and an XPCB association motif, overview Mus musculus

Synonyms

Synonyms Comment Organism
peptide N-glycanase
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Mus musculus
PNGase
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Mus musculus