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IUBMB Comments This enzyme is part of the pathway from urate to (S )-allantoin, which is present in bacteria, plants and animals (but not in humans).
Synonyms
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OHCU decarboxylase
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5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)-allantoin + CO2
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MetaCyc
urate conversion to allantoin I, urate conversion to allantoin II, urate conversion to allantoin III
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5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate carboxy-lyase [(S)-allantoin-forming]
This enzyme is part of the pathway from urate to (S)-allantoin, which is present in bacteria, plants and animals (but not in humans).
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5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
Substrates: -
?
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
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Substrates: -
?
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
Substrates: -
?
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
Substrates: -
?
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
Substrates: the enzyme is part of the pathway from urate to (S)-allantoin
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
Substrates: -
?
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
-
Substrates: -
?
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
Substrates: -
?
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
(S)-allantoin + CO2
Substrates: the enzyme is part of the pathway from urate to (S)-allantoin
?
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allopurinol
competitive inhibitor. The inhibitor disrupts the necessary organization of the active site
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Gout
The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides insights into the mechanism of uric acid degradation.
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0.151
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
mutant enzyme Q88E, pH and temperature not specified in the publication
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122
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
mutant enzyme Q88E, pH and temperature not specified in the publication
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19 - 970
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
19
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
mutant enzyme Q88E, pH and temperature not specified in the publication
970
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
wild-type enzyme, pH and temperature not specified in the publication
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0.03
allopurinol
mutant enzyme Q88E, pH and temperature not specified in the publication
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SwissProt
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SwissProt
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UniProt
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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malfunction
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an uro3 deletion mutant exhibits growth defects on uric acid, but displays wild type growth on allantoin, urea and ammonium
physiological function
the enzyme is part of the pathway from urate to (S)-allantoin
physiological function
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the enzyme is dispensable for virulence
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homodimer
x-ray crystallography
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hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.5), 20 mM MgCl2, and 16% (w/v) polyacrylic acid 5100, at 22°C
sitting drop vapor diffusion method, using 20% (v/v) EtOH, 100 mM Tris-HCl, pH 8.5
hanging-drop vapor-diffusion method at 18°C
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Q88E
the maximal rate of this mutant is 43fold slower than that of the native rate, whereas the measured Km for the mutant is similar to that of the native enzyme, the kcat/Km value is about 50fold lower than the wild-type value
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immobilized metal affinity chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli BL21-CodonPlus(DE3) cells
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French, J.B.; Ealick, S.E.
Structural and mechanistic studies on Klebsiella pneumoniae 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
J. Biol. Chem.
285
35446-35454
2010
Klebsiella pneumoniae (A6T925), Klebsiella pneumoniae
brenda
Cendron, L.; Berni, R.; Folli, C.; Ramazzina, I.; Percudani, R.; Zanotti, G.
The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides insights into the mechanism of uric acid degradation
J. Biol. Chem.
282
18182-18189
2007
Danio rerio (A1L259)
brenda
Kim, K.; Park, J.; Rhee, S.
Structural and functional basis for (S)-allantoin formation in the ureide pathway
J. Biol. Chem.
282
23457-23464
2007
Arabidopsis thaliana (Q9LVM5)
brenda
Lee, I.R.; Yang, L.; Sebetso, G.; Allen, R.; Doan, T.H.; Blundell, R.; Lui, E.Y.; Morrow, C.A.; Fraser, J.A.
Characterization of the complete uric acid degradation pathway in the fungal pathogen Cryptococcus neoformans
PLoS ONE
8
e64292
2013
Cryptococcus neoformans
brenda
Transporter Classification Database (TCDB):
9.B.35.1.3
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