This enzyme was previously thought to be a copper protein, but it is now known that the enzymes from soy bean (Glycine max), the mould Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO2, although there is an enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate hydrolase, catalyses the first step. The enzyme is different from EC 1.14.13.113 (FAD-dependent urate hydroxylase).
The taxonomic range for the selected organisms is: Arthrobacter globiformis The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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SYSTEMATIC NAME
IUBMB Comments
urate:oxygen oxidoreductase
This enzyme was previously thought to be a copper protein, but it is now known that the enzymes from soy bean (Glycine max), the mould Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO2, although there is an enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate hydrolase, catalyses the first step. The enzyme is different from EC 1.14.13.113 (FAD-dependent urate hydroxylase).
determined by X-ray diffraction measurements, the AgUOX-native structure is solved by molecular replacement using the program AmoRe, pairs of dimers are stacked face-to-face to form a tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
the mutations introduce disulfide bonds between the subunits and markedly increase the melting temperature (from 61 to 75°C) of the enzyme compared with wild type
the mutations introduce disulfide bonds between the subunits and markedly increase the melting temperature (from 61 to 70°C) of the enzyme compared with wild type
expression in Escherichia coli, Escherichia coli harboring pUOD1 produces 20fold higher uricase than the original Arthrobacter strain, even without an inducer