3.5.2.17: hydroxyisourate hydrolase
This is an abbreviated version!
For detailed information about hydroxyisourate hydrolase, go to the full flat file.
Word Map on EC 3.5.2.17
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3.5.2.17
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amyloidosis
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amyloid
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polyneuropathy
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cardiac
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fibril
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hereditary
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cardiomyopathy
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amyloidogenic
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neuropathy
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thyroxin
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albumin
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retinol
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tetramer
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nerve
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retinol-binding
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apolipoproteins
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senile
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alzheimer
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immunoglobulin
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cerebrospinal
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misfolding
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plexus
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scintigraphy
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ventricular
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choroid
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transferrin
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vitreous
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haptoglobin
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congo
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carpal
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amyloidogenesis
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echocardiography
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malnutrition
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late-onset
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prealbumin
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ejection
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light-chain
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csf
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endomyocardial
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medicine
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fibrillogenesis
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homotetrameric
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leptomeningeal
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gammopathy
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sensorimotor
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deiodinase
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orthostatic
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sural
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dysautonomia
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non-amyloidogenic
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portuguese
- 3.5.2.17
- amyloidosis
-
amyloid
- polyneuropathy
- cardiac
-
fibril
- hereditary
- cardiomyopathy
-
amyloidogenic
- neuropathy
- thyroxin
- albumin
- retinol
- tetramer
- nerve
-
retinol-binding
-
apolipoproteins
-
senile
- alzheimer
- immunoglobulin
-
cerebrospinal
- misfolding
- plexus
-
scintigraphy
- ventricular
- choroid
- transferrin
-
vitreous
- haptoglobin
-
congo
-
carpal
-
amyloidogenesis
-
echocardiography
- malnutrition
-
late-onset
-
prealbumin
-
ejection
- light-chain
- csf
-
endomyocardial
- medicine
-
fibrillogenesis
-
homotetrameric
- leptomeningeal
- gammopathy
-
sensorimotor
-
deiodinase
-
orthostatic
-
sural
- dysautonomia
-
non-amyloidogenic
-
portuguese
Reaction
Synonyms
5-HIUase, 5-hydroxyisourate hydrolase, ecTRP, HIU, HIU hydrolase, HIUase, HIUHase, HIUHase 1, hTTR, hydroxyisourate hydrolase, PucM, sbTTR, TLP, transthyretin, transthyretin-like protein, transthyretin-related protein, TRP, TTL, Urah
ECTree
3.5.2.17 hydroxyisourate hydrolaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.2.17 - hydroxyisourate hydrolase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-hydroxyisourate + H2O
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
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-
-
?
5-hydroxyisourate + H2O
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
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-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
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enzyme shows 5-hydroxyisourate hydrolase and 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activities in vitro
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-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
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-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
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-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
-
-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
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-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
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-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
-
-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
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ureide pathway
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?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
-
-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
-
-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
-
-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
-
-
-
-
?
additional information
?
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reaction is likely to be initiated by a water molecule that is first activated by deprotonation. The hydrogen-bonding interactions between the water molecule and residues His7 and His92 would serve to orient the water ideally for attack at C6 of the purine ring. The C-terminal serine residue, Ser108, is in position to form a hydrogen bond to His7 and may indirectly participate in catalysis by inductively activating this residue. Deprotonation of the water by His7 creates a hydroxide nucleophile that attacks C6 of the purine ring, leading to a tetrahedral oxyanion intermediate. The charge on the resulting oxyanion would be stabilized by the positively charged guanidinium group of Arg41. Arg41 from the neighboring chain helps to stabilize the charge on the oxyanion intermediate.Collapse of the oxyanion would then lead to ring opening, with the final proton coming from the nearby Arg41. The original proton abstracted from a water molecule by His7 would then be transferred to Arg41 to complete the catalytic cycle
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-
?
additional information
?
-
-
reaction is likely to be initiated by a water molecule that is first activated by deprotonation. The hydrogen-bonding interactions between the water molecule and residues His7 and His92 would serve to orient the water ideally for attack at C6 of the purine ring. The C-terminal serine residue, Ser108, is in position to form a hydrogen bond to His7 and may indirectly participate in catalysis by inductively activating this residue. Deprotonation of the water by His7 creates a hydroxide nucleophile that attacks C6 of the purine ring, leading to a tetrahedral oxyanion intermediate. The charge on the resulting oxyanion would be stabilized by the positively charged guanidinium group of Arg41. Arg41 from the neighboring chain helps to stabilize the charge on the oxyanion intermediate.Collapse of the oxyanion would then lead to ring opening, with the final proton coming from the nearby Arg41. The original proton abstracted from a water molecule by His7 would then be transferred to Arg41 to complete the catalytic cycle
-
-
?
additional information
?
-
reaction is likely to be initiated by a water molecule that is first activated by deprotonation. The hydrogen-bonding interactions between the water molecule and residues His7 and His92 would serve to orient the water ideally for attack at C6 of the purine ring. The C-terminal serine residue, Ser108, is in position to form a hydrogen bond to His7 and may indirectly participate in catalysis by inductively activating this residue. Deprotonation of the water by His7 creates a hydroxide nucleophile that attacks C6 of the purine ring, leading to a tetrahedral oxyanion intermediate. The charge on the resulting oxyanion would be stabilized by the positively charged guanidinium group of Arg41. Arg41 from the neighboring chain helps to stabilize the charge on the oxyanion intermediate.Collapse of the oxyanion would then lead to ring opening, with the final proton coming from the nearby Arg41. The original proton abstracted from a water molecule by His7 would then be transferred to Arg41 to complete the catalytic cycle
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-
?
