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 (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 | Organism |
---|---|
zinc binding stabilizes the enzyme conformation by stabilizing the intermediate state and promoting product release | Mus musculus |
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 | 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 | 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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
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 | 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 | 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 | ? | - |
? |
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 | Comment | Organism |
---|---|---|
peptide N-glycanase | - |
Mus musculus |
PNGase | - |
Mus musculus |