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Literature summary extracted from

  • Juan, E.; Hoque, M.; Shimizu, S.; Hossain, M.; Yamamoto, T.; Imamura, S.; Suzuki, K.; Tsunoda, M.; Amano, H.; Sekiguchi, T.; Takenaka, A.
    Structures of Arthrobacter globiformis urate oxidase-ligand complexes (2008), ACTA CRYSTALLOGR. SECT. D, 64, 815-822.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.3.3 a plasmid containing the AgUOX gene is introduced into the expression host cell Escherichia coli DH1 Arthrobacter globiformis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
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 Arthrobacter globiformis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.3.3 8-Azaxanthine substrate analogue Arthrobacter globiformis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.3.3 urate + O2 + H2O Arthrobacter globiformis ureide pathway 5-hydroxyisourate + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.7.3.3 Arthrobacter globiformis D0VWQ1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.3.3 by anion exchange and hydropbobic interaction chromatography Arthrobacter globiformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.3.3 urate + O2 + H2O ureide pathway Arthrobacter globiformis 5-hydroxyisourate + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.3.3 homotetramer 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 Arthrobacter globiformis

Synonyms

EC Number Synonyms Comment Organism
1.7.3.3 AgUOX
-
 Arthrobacter globiformis
1.7.3.3 Urate oxidase
-
 Arthrobacter globiformis
1.7.3.3 uricase
-
 Arthrobacter globiformis

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.3.3 additional information UOX is unique among the oxygen-requiring enzymes in the sense that it does not need a cofactor to convert uric acid to 5-hydroxyisourate Arthrobacter globiformis