EC Number   |
Reference |
|---|
    1.7.3.3 | - |
658316 |
| 1.7.3.3 | crystallization of large proteins in the presence of polyethylene glycol |
394191 |
| 1.7.3.3 | crystallizations are performed using the hanging-drop vapour-diffusion method at 19.9°C, structures of crystals soaked with the substrate uric acid, the inhibitor 8-azaxanthin and allantoin are determined at 1.9-2.2 A resolution, 2 homotetramers comprise the asymmetric crystallographic unit, each subunit contains 2 T-fold domains of topology, which are usually found in purine- and pterin-binding enzymes, the uric acid substrate is bound tightly to the enzyme by interactions with Arg180, Leu222 and Gln223 from one subunit and with Thr67 and sp68 of the neighbouring subunit in the tetramer |
695394 |
| 1.7.3.3 | crystals of about a few tens of micrometres in size, which is nucleated previously in crystallization batch containing 5% PEG 8000, 100 mM NaCl, 8 mg/ml uox-substrate complex and 100 mM Tris-HCl pH 8.5, are used as seeds and their size and quality are further improved using a temperature-control device, large crystals of Uox, co-crystallized with its substrates analogues 8-azaxanthine, 9-methyluric acid or the natural substrate in the presence of cyanide (0.5-2 mg/ml), and soaks with the natural substrate in the absence of cyanide, diffracting to high resolutions are obtained, in the presence of different inhibitors, the crystal form of Uox has a body-centred orthorhombic symmetry and one of the largest primitive unit-cell volumes (a: 80 A, b: 96 A, c: 106 A) |
699832 |
| 1.7.3.3 | enzyme in complex with substrate urate and inhibitor cyanide, X-ray diffraction structure determination and analysis |
697005 |
| 1.7.3.3 | hanging drop vapour diffusion method |
672398 |
| 1.7.3.3 | homology modeling of monomeric enzyme. The highly conserved residue Gly290 could interact with Asn262 and His264. Residue substitutions near Gly290 may affect its spatial orientation and result in changes in catalysis.Gly290 is likely to participate in the structure of the active site and to be involved in oxygen-binding |
724483 |
| 1.7.3.3 | ligand-free Uox crystallized with NH4Cl and 15% (w/v) PEG 8000, ligand-free Uox crystallized in water with 10% (w/v) PEG 8000, ligand-free Uox crystallized with NaCl and 15% (w/v) PEG 8000, ligand-free Uox crystallized with (NH4)2SO4 and 15% (w/v) PEG 8000, ligand-free Uox crystallized with NaCl and 8% PEG 8000, ligand-free Uox crystallized with KCl and 10% (w/v) PEG 8000, and Uox complexed with 8-azaxanthine and crystallized with NaCl and 10% (w/v) PEG 8000, in 50 mM Tris buffer pH 8.0 |
710719 |
| 1.7.3.3 | mutant enzyme K12C/E286C, sitting drop vapor diffusion method, using 12% (w/v) polyethylene glycol 3350 and 0.1 M sodium malonate (pH 5.0) |
763852 |
| 1.7.3.3 | quantum mechanical/molecular mechanical calculations based on PDB entry 4N9M. The oxidation consists of chemical transformation from 8-hydroxyxythine to an anionic radical via a proton transfer along with an electron transfer, proton transfer to the O2- anion (radical), diradical recombination to form a peroxo intermediate, and dissociation of H2O2 to generate the dehydrourate. Hydration is initiated by the nucleophilic attack of a water molecule on dehydrourate, along with a concerted proton transfer through residue Thr69 in the catalytic site. Hydration is the rate-determining step |
741486 |
