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Information on EC 3.5.2.17 - hydroxyisourate hydrolase
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3.5.2.17 hydroxyisourate hydrolaseIUBMB Comments
The reaction is the first stage in the conversion of 5-hydroxyisourate into S-allantoin. This reaction will also occur spontaneously but more slowly.
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Word Map
- 3.5.2.17
- amyloidosis
- polyneuropathy
- fibril
-
amyloidogenic
- hereditary
- neuropathy
-
thyroxin
- retinol
- cardiomyopathy
-
retinol-binding
-
apolipoproteins
- nerve
- alzheimer
- choroid
- plexus
-
cerebrospinal
-
senile
-
val30met
-
transferrin
- misfolding
-
prealbumin
-
c-reactive
-
globulin
-
late-onset
-
light-chain
-
carpal
-
homotetrameric
- malnutrition
-
congo
-
portuguese
-
amyloidogenesis
-
vitreous
-
haptoglobin
-
scintigraphy
-
orosomucoid
-
non-amyloidogenic
-
blood-cerebrospinal
-
deiodinase
- leptomeningeal
-
gelsolin
-
protein-energy
-
endomyocardial
- dysautonomia
- medicine
-
pbdes
-
fibrillogenesis
-
sensorimotor
-
sural
-
hormone-binding
-
echocardiographic
-
orthostatic
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
transthyretin, transthyretin-like protein, 5-hydroxyisourate hydrolase, transthyretin-related protein, hiu hydrolase, hiuhase, hiuase, sbttr, ectrp, hiuhase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-hydroxyisourate hydrolase
HIU
HIUHase
hydroxyisourate hydrolase
transthyretin
transthyretin-related protein
5-hydroxyisourate hydrolase
-
-
-
-
HIUHase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
The reaction is the first stage in the conversion of 5-hydroxyisourate into S-allantoin. This reaction will also occur spontaneously but more slowly
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
5-hydroxyisourate amidohydrolase
The reaction is the first stage in the conversion of 5-hydroxyisourate into S-allantoin. This reaction will also occur spontaneously but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
255885-20-2
-
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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
-
-
-
?
5-hydroxyisourate + H2O
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
-
-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
-
enzyme shows 5-hydroxyisourate hydrolase and 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activities in vitro
-
-
?
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
-
-
-
?
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
-
ureide pathway
-
?
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
?
-
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
-
-
-
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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NATURAL SUBSTRATE
NATURAL 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
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
Q8S3J3
-
-
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
-
ureide pathway
-
?
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
U6C7K1
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the enzyme is not affected by 1 mM of Cr3+, Mg2+, or Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
5-hydroxyisourate
pH 7.5, 37°C, recombinant enzyme lacking the signal peptide
0.093
5-hydroxyisourate
mutant S108A, pH 7.6, temperature not specified in the publication
0.103
5-hydroxyisourate
wild-type, pH 7.6, temperature not specified in the publication
0.195
5-hydroxyisourate
mutant R41K, pH 7.6, temperature not specified in the publication
0.43
5-hydroxyisourate
mutant H92N, pH 7.6, temperature not specified in the publication
4.4
5-hydroxyisourate
mutant H7N, pH 7.6, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35
5-hydroxyisourate
mutant H92N, pH 7.6, temperature not specified in the publication
0.8
5-hydroxyisourate
mutant H7N, pH 7.6, temperature not specified in the publication
24
5-hydroxyisourate
pH 7.5, 37°C, recombinant enzyme lacking the signal peptide
34.7
5-hydroxyisourate
mutant R41K, pH 7.6, temperature not specified in the publication
81
5-hydroxyisourate
mutant S108A, pH 7.6, temperature not specified in the publication
172
5-hydroxyisourate
wild-type, pH 7.6, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.18
5-hydroxyisourate
mutant H7N, pH 7.6, temperature not specified in the publication
0.82
5-hydroxyisourate
mutant H92N, pH 7.6, temperature not specified in the publication
180
5-hydroxyisourate
mutant R41K, pH 7.6, temperature not specified in the publication
870
5-hydroxyisourate
mutant S108A, pH 7.6, temperature not specified in the publication
1700
5-hydroxyisourate
wild-type, pH 7.6, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the 5-hydroxyisourate hydrolase/transthyretin superfamily: evolutionary and functional analyses, overview. Teleosts have highly diverged genomes that resulted from whole genome duplication, which leads to an extensive diversity of paralogous genes. Transthyretin, an extracellular thyroid hormone binding protein, is thought to have evolved from an ancestral 5-hydroxyisourate hydrolase by gene duplication at some stage of chordate evolution. Phylogenetic analysis of the teleost aa sequences reveals the presence of two HIUHase subfamilies, HIUHase 1 (which has an N-terminal peroxisomal targeting signal-2) and HIUHase 2 (which does not have an N-terminal PTS2), and one transthyretin family
metabolism
the enzyme catalyzes the hydrolysis of 5-hydroxyisourate in the purine degradation pathway, and transthyretin, a thyroid hormone binding protein
physiological function
-
point mutation Y98Cin the gene encoding mouse HIU hydrolase, Urah, results in undetectable protein expression. Mice homozygous for this mutation develop elevated platelet counts secondary to excess thrombopoietin production and hepatomegaly. The majority of homozygous mutant mice also develop hepatocellular carcinoma, and tumor development is accelerated by exposure to radiation
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12439
-
x * 12439, calculated, x * 15000, SDS-PAGE of recombinant protein
15000
-
x * 12439, calculated, x * 15000, SDS-PAGE of recombinant protein
68000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 12439, calculated, x * 15000, SDS-PAGE of recombinant protein
homotetramer
tetramer
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
at 4°C by the sitting-drop, vapour diffusion method, using 0.1 M HEPES (pH 7.5), 20% (w/v) PEG 10000
-
mutants Y116T, I16A/Y116T and mutant I16A/Y116T in complex with thyroxine, to 1.7 A, 2.3 A., and 1.95 A resoultion. Structural comparison of HIUase and transthyretin, TTR. Mutations Y116T and I16A are likely to be crucial events in order to induce, after a gene duplication event, the conversion of the enzyme HIUase into a binding protein, transthyretin. The mutations at the active sites of HIUase open up the two ends of the channel that transverses the entire tetrameric protein, generating two cavities accessible to the thyroxine molecule and abrogating, at the same time, the enzymatic activity
-
to 1.8 A resolution, and modeling of substrate 5-hydroxyisourate into the active site. The four chains of the enzyme come together to form a homotetramer with 222 symmetry. The tetramer is a dimer of dimers, with two protomers arranged to create an extended beta-sheet that makes up the dimer–dimer interface
hanging drop vapour diffusion method in 0.1 M sodium cacodylate (pH 6.0), 0.2 M MgCl2, 20% (w/v) polyethylene glycol 3350 at 22°C
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I16A
-
mutation at the active sites of HIUase, opens up one end of the channel that transverses the entire tetrameric protein, generating a cavity accessible to the thyroxine molecule and abrogating, at the same time, the enzymatic activity
I16A/Y116T
-
mutations at the active sites of HIUase open up the two ends of the channel that transverses the entire tetrameric protein, generating two cavities accessible to the thyroxine molecule and abrogating, at the same time, the enzymatic activity
Y116T
-
mutation at the active sites of HIUase, opens up one end of the channel that transverses the entire tetrameric protein, generating a cavity accessible to the thyroxine molecule and abrogating, at the same time, the enzymatic activity
E199A
E408A
Y98C
-
point mutation in the gene encoding mouse HIU hydrolase, Urah, that perturbes uric acid metabolism within the liver. The substitution of cysteine for tyrosine in a conserved helical region results in undetectable protein expression. Mice homozygous for this mutation develop elevated platelet counts secondary to excess thrombopoietin production and hepatomegaly. The majority of homozygous mutant mice also develop hepatocellular carcinoma, and tumor development is accelerated by exposure to radiation
additional information
the deletion mutation DELTAYRGS greatly affects activity
E199A
site-directed mutagenesis, mutant devoid of detectable catalytic activity
E408A
site-directed mutagenesis, mutant devoid of detectable catalytic activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant soluble His-tagged enzyme from Escherichia coli by metal affinity chromatography
Superose-12 gel filtration and HiTrap SP column chromatography
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta BL21 cells
-
expression in Escherichia coli
expression in Escherichia coli strain BL21
phylogenetic analysis, sequence comparisons, quantitative real-time PCR enzyme expression analysis, recombinant expression of soluble His-tagged enzyme in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
point mutation Y98Cin the gene encoding mouse HIU hydrolase, Urah, results in undetectable protein expression. Mice homozygous for this mutation develop elevated platelet counts secondary to excess thrombopoietin production and hepatomegaly. The majority of homozygous mutant mice also develop hepatocellular carcinoma, and tumor development is accelerated by exposure to radiation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Raychaudhuri, A.; Tipton, P.A.
A familiar motif in a new context: the catalytic mechanism of hydroxyisourate hydrolase
Biochemistry
42
6848-6852
2003
Glycine max
brenda
Raychaudhuri, A.; Tipton, P.A.
Cloning and expression of the gene for soybean hydroxyisourate hydrolase. Localization and implications for function and mechanism
Plant Physiol.
130
2061-2068
2002
Glycine max, Glycine max (Q8S3J3)
brenda
Sarma, A.D.; Serfozo, P.; Kahn, K.; Tipton, P.A.
Identification and purification of hydroxyisourate hydrolase, a novel ureide-metabolizing enzyme
J. Biol. Chem.
274
33863-33865
1999
Glycine max
brenda
Jung, D.K.; Lee, Y.; Park, S.G.; Park, B.C.; Kim, G.H.; Rhee, S.
Structural and functional analysis of PucM, a hydrolase in the ureide pathway and a member of the transthyretin-related protein family
Proc. Natl. Acad. Sci. USA
103
9790-9795
2006
Bacillus subtilis, Bacillus subtilis (O32142)
brenda
Hennebry, S.C.; Law, R.H.; Richardson, S.J.; Buckle, A.M.; Whisstock, J.C.
The crystal structure of the transthyretin-like protein from Salmonella dublin, a prokaryote 5-hydroxyisourate hydrolase
J. Mol. Biol.
359
1389-1399
2006
Salmonella enterica subsp. enterica serovar Dublin
brenda
Zanotti, G.; Cendron, L.; Ramazzina, I.; Folli, C.; Percudani, R.; Berni, R.
Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter
J. Mol. Biol.
363
1-9
2006
Danio rerio, Danio rerio (Q06S87)
brenda
Lee, Y.; Park, B.C.; Lee, d.o..H.; Bae, K.H.; Cho, S.; Lee, C.H.; Lee, J.S.; Myung, P.K.; Park, S.G.
Mouse transthyretin-related protein is a hydrolase which degrades 5-hydroxyisourate, the end product of the uricase reaction
Mol. Cell
22
141-145
2006
Mus musculus, Mus musculus (Q9CRB3)
brenda
Lundberg, E.; Olofsson, A.; Westermark, G.T.; Sauer-Eriksson, A.E.
Stability and fibril formation properties of human and fish transthyretin, and of the Escherichia coli transthyretin-related protein
FEBS J.
276
1999-2011
2009
Chilotilapia rhoadesii, Escherichia coli, Escherichia coli (P76341), Homo sapiens
brenda
Matiollo, C.; Vernal, J.; Ecco, G.; Bertoldo, J.B.; Razzera, G.; de Souza, E.M.; Pedrosa, F.O.; Terenzi, H.
A transthyretin-related protein is functionally expressed in Herbaspirillum seropedicae
Biochem. Biophys. Res. Commun.
387
712-716
2009
Herbaspirillum seropedicae
brenda
Pessoa, J.; Sarkany, Z.; Ferreira-da-Silva, F.; Martins, S.; Almeida, M.; Li, J.; Damas, A.
Functional characterization of Arabidopsis thaliana transthyretin-like protein
BMC Plant Biol.
10
30
2010
Arabidopsis thaliana
brenda
Stevenson, W.S.; Hyland, C.D.; Zhang, J.G.; Morgan, P.O.; Willson, T.A.; Gill, A.; Hilton, A.A.; Viney, E.M.; Bahlo, M.; Masters, S.L.; Hennebry, S.; Richardson, S.J.; Nicola, N.A.; Metcalf, D.; Hilton, D.J.; Roberts, A.W.; Alexander, W.S.
Deficiency of 5-hydroxyisourate hydrolase causes hepatomegaly and hepatocellular carcinoma in mice
Proc. Natl. Acad. Sci. USA
107
16625-16630
2010
Mus musculus
brenda
French, J.B.; Ealick, S.E.
Structural and kinetic insights into the mechanism of 5-hydroxyisourate hydrolase from Klebsiella pneumoniae
Acta Crystallogr. Sect. D
67
671-677
2011
Klebsiella pneumoniae (A6T926), Klebsiella pneumoniae, Klebsiella pneumoniae ATCC 700721 (A6T926)
brenda
Cendron, L.; Ramazzina, I.; Percudani, R.; Rasore, C.; Zanotti, G.; Berni, R.
Probing the evolution of hydroxyisourate hydrolase into transthyretin through active-site redesign
J. Mol. Biol.
409
504-512
2011
Danio rerio (Q06S87)
brenda
Kasai, K.; Nishiyama, N.; Yamauchi, K.
Characterization of Oncorhynchus mykiss 5-hydroxyisourate hydrolase/transthyretin superfamily: evolutionary and functional analyses
Gene
531
326-336
2013
Oncorhynchus mykiss, Oncorhynchus mykiss (U6C7K1)
brenda
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