Literature summary for 1.7.3.3 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.

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Inhibitors	Comment	Organism	Structure
8-Azaxanthine	substrate analogue	Arthrobacter globiformis

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Arthrobacter globiformis	D0VWQ1	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
AgUOX	-	Arthrobacter globiformis
Urate oxidase	-	Arthrobacter globiformis
uricase	-	Arthrobacter globiformis

Cofactor

Cofactor	Comment	Organism	Structure
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