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2.3.2.5: glutaminyl-peptide cyclotransferase

This is an abbreviated version!
For detailed information about glutaminyl-peptide cyclotransferase, go to the full flat file.

Word Map on EC 2.3.2.5

Reaction

L-glutaminyl-peptide
=
5-Oxoprolyl-peptide
 +
NH3

Synonyms

AtQC, cyclotransferase, glutaminyl-transfer ribonucleate, DromeQC, gamma-glutamylamine cyclotransferase, GGACT, glutamine cyclotransferase, glutaminyl cyclase, glutaminyl-peptide cyclotransferase-like protein, glutaminyl-tRNA cyclotransferase, golgi resident enzyme, Golgi resident glutaminyl cyclase, Golgi-resident enzyme, Golgi-resident glutaminyl cyclase, gQC, h-isoQC, h-QC, hQC, isoDromeQC, isoGlutaminyl cyclase, isoQC, PgQC, QC, QCT, Qpct, Qpct1, QPCTL, secretory glutaminyl cyclase, sQC, StQC

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.5 glutaminyl-peptide cyclotransferase

Crystallization

Crystallization on EC 2.3.2.5 - glutaminyl-peptide cyclotransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters A = 62.82 A, b = 81.23 A, c = 108.17 A and two molecules per asymmetric unit, resolution 1.7 A
-
hatbox-shaped molecule that forms an unusual five-fold beta-propeller traversed by a central channel
structure determinantion by single wavelength anomalous diffraction technique using sulfur and zinc as anomalous scatterers. The zinc ion present is bound via an octahedral coordination into an elongated cavity along the pseudo 5fold axis of the beta-propeller fold. The active site is located at the C-terminal entrance of the enzyme’s central tunnel with residues W83, W110, Q24, E69, N155, K225, F22, and F67 in the entrance
hanging drop vapor diffusion method, using 10% (w/v) PEG 35000 and 100 mM Tris (pH 8.5) for isoform DromeQC
hanging drop vapor diffusion method, using 200 mM MnCl2, 30% (w/v) PEG 4000, and 100 mM Tris (pH 8.5) for isoform isoDromeQC
analysis of 23 human sQC structures, diverse PDB IDs, overview
analysis of several human gQC structures, i.e. PDB IDs 3PB4, 3PB6, 3PB7, 3PB8, and 3PB9, overview
hanging drop vapor diffusion method, using 100 mM imidazole (pH 8.0), 30% (v/v) 2-methyl-2,4-pentanediol, and 11% (w/v) 4000 PEG
hanging drop vapor-diffusion method. The space group of the crystal is R32, with typical unit cells of a = b = 119 A and c = 333A, in which an asymmetric unit comprises two human glutaminyl cyclase molecules. Crystal structures of the enzyme bound to inhibitors: 1-vinylimidazole, 1-benzylimidazole and N-omega-acetylhistamine
hanging-drop vapor diffusion
-
mutant enzyme W207F, hanging drop vapor diffusion method, using 1.7 M (NH4)2SO4, 4% (v/v) dioxane, and 100 mM MES, pH 6.5, at 25°C
purified recombinant His-tagged enzyme double mutant Y115E/Y117E in complex with inhibitor SEN177 and Zn2+, vapor diffusion technique, mixing an equal volume of protein sample and precipitant solution, X-ray diffraction structure determination and analysis at 1.72 A resolution, molecular replacement with the structure PDB ID 4YU9 as template, modeling
sitting drop vapor diffusion method, using either 30% (w/v) PEG 200, 5% (w/v) PEG 3000, and 0.1 M MES, pH 6.0, or 50% (w/v) PEG 200, 0.2 M MgCl2, and 0.1 M cacodylate, pH 6.5
sitting drop vapor diffusion method, using 10% (w/v) PEG 8000, 8% (v/v) ethylene glycol, 0.1 M HEPES pH 7.5
hanging drop vapor diffusion method, using 100 mM sodium acetate (pH 5.3), 200 mM ammonium sulfate, and 12% (w/v) 2000 MME-PEG
hanging drop vapor diffusion method, using 0.1 M MES and 30% (w/v) PEG-4000
mutant enzyme E89A, hanging drop vapor diffusion method, using 50 mM imidazole and 0.8 M sodium citrate, pH 8.7, at 25°C
hanging drop vapor diffusion method, using 0.1 M sodium acetate pH 4.6, 0.2 M ammonium sulfate and 12% (w/v) PEG-4000