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50% inhibition of ferricyanide reduction in xanthine oxidation assay at 5 mM
-
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
anion-pi interactions are present in the active site of the enzyme and are energetically favorable. Uric acid and 8-azaxanthine are able to interact favorably with cyanide and chloride ions, respectively and both uric acid and 8-azaxanthine react with water
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
competitive inhibitor, binding structure, overview
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
substrate analogue binds in the active site of the enzyme
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Uricase of Bacillus fastidiosus. Properties and regulation of synthesis
1978
Bongaerts, G.P.A.; Uitzetter, J.; Brouns, R.; Vogels, G.D.
Biochim. Biophys. Acta
527
348-358
Xanthine phosphoribosyltransferase from Streptococcus faecalis. Properties and specificity
1974
Miller, R.L.; Adamczyk, D.L.; Fyfe, J.A.; Elion, G.B.
Arch. Biochem. Biophys.
165
349-358
Purification and properties of trans-N-deoxyribosylase
1958
Roush, A.H.; Betz, R.F.
J. Biol. Chem.
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trans-N-Deoxyribosylase: substrate specificity studies. Purine bases as acceptors
1975
Holguin, J.; Cardinaud, R.
Eur. J. Biochem.
54
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Purification and substrate inactivation of xanthine dehydrogenase from Chlamydomonas reinhardtii
1992
Perez-Vicente, R.; Alamillo, J.M.; Cardenas, J.; Pineda, M.
Biochim. Biophys. Acta
1117
159-166
Purification and properties of xanthine dehydrogenase from Micrococcus lactilyticus
1967
Smith, S.T.; Rajagopalan, K.V.; Handler, P.
J. Biol. Chem.
242
4108-4117
-
Molecular and kinetic characterization of xanthine dehydrogenase from the phototrophic bacterium Rodopseudomonas capsulata
1981
Aretz, W.; Kaspari, H.; Klemme, J.H.
Z. Naturforsch. C
36
933-941
-
Purification, crystallization, and some properties of xanthine dehydrogenase from Pseudomonas synxantha A 3
1979
Sakai, T.; Jun, H.K.
Agric. Biol. Chem.
43
753-760
High pressure macromolecular crystallography: The 140-MPa crystal structure at 2.3 A resolution of urate oxidase, a 135-kDa tetrameric assembly
2006
Colloch, N.; Girard, E.; Dhaussy, A.; Kahn, R.; Ascone, I.; Mezouar, M.; Fourme, R.
Biochim. Biophys. Acta
1764
391-397
Structures of Arthrobacter globiformis urate oxidase-ligand complexes
2008
Juan, E.; Hoque, M.; Shimizu, S.; Hossain, M.; Yamamoto, T.; Imamura, S.; Suzuki, K.; Tsunoda, M.; Amano, H.; Sekiguchi, T.; Takenaka, A.
ACTA CRYSTALLOGR. SECT. D
64
815-822
Oxygen pressurized X-ray crystallography: probing the dioxygen binding site in cofactorless urate oxidase and implications for its catalytic mechanism
2008
Colloc'h, N.; Gabison, L.; Monard, G.; Altarsha, M.; Chiadmi, M.; Marassio, G.; Sopkova-de Oliveira Santos, J.; El Hajji, M.; Castro, B.; Abraini, J.H.; Prange, T.
Biophys. J.
95
2415-2422
Large crystal growth by thermal control allows combined X-ray and neutron crystallographic studies to elucidate the protonation states in Aspergillus flavus urate oxidase
2009
Oksanen, E.; Blakeley, M.P.; Bonnete, F.; Dauvergne, M.T.; Dauvergne, F.; Budayova-Spano, M.
J. R. Soc. Interface
6 Suppl 5
599-610
Polymorphism of microcrystalline urate oxidase from Aspergillus flavus
2010
Collings, I.; Watier, Y.; Giffard, M.; Dagogo, S.; Kahn, R.; Bonnete, F.; Wright, J.P.; Fitch, A.N.; Margiolaki, I.
Acta Crystallogr. Sect. D
66
539-548
Novel insights for dihydroorotate dehydrogenase class 1A inhibitors discovery
2010
Cheleski, J.; Rocha, J.R.; Pinheiro, M.P.; Wiggers, H.J.; da Silva, A.B.; Nonato, M.C.; Montanari, C.A.
Eur. J. Med. Chem.
45
5899-5909
Relevant anion-Ï interactions in biological systems: The case of urate oxidase
2011
Estarellas, C.; Frontera, A.; Quinonero, D.; Deya, P.
Angew. Chem. Int. Ed. Engl.
50
415-418
Arxula adeninivorans recombinant guanine deaminase and its application in the production of food with low purine content
2014
Trautwein-Schult, A.; Jankowska, D.; Cordes, A.; Hoferichter, P.; Klein, C.; Matros, A.; Mock, H.P.; Baronian, K.; Bode, R.; Kunze, G.
J. Mol. Microbiol. Biotechnol.
24
67-81
Biochemical characterization of Kluyveromyces lactis adenine deaminase and guanine deaminase and their potential application in lowering purine content in beer
2018
Mahor, D.; Prasad, G.S.
Front. Bioeng. Biotechnol.
6
180