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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
-
amyloid
- polyneuropathy
- cardiac
-
fibril
- hereditary
-
amyloidogenic
- cardiomyopathy
- neuropathy
- thyroxin
- albumin
-
apolipoproteins
-
retinol-binding
- tetramer
- retinol
- nerve
- alzheimer
- csf
-
senile
- ventricular
- plexus
- misfolding
-
cerebrospinal
- choroid
-
carpal
- malnutrition
-
amyloidogenesis
-
late-onset
-
scintigraphy
-
echocardiography
- light-chain
-
congo
-
portuguese
- haptoglobin
- transferrin
-
vitreous
-
prealbumin
- dysautonomia
-
protofilaments
- medicine
-
deiodinase
-
protein-energy
-
homotetrameric
-
endomyocardial
-
non-amyloidogenic
-
orthostatic
- gammopathy
-
fibrillogenesis
-
sensorimotor
- leptomeningeal
-
sural
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
5-HIUase, 5-hydroxyisourate hydrolase, ecTRP, HIU, HIU hydrolase, HIUase, HIUHase, HIUHase 1, hTTR, hydroxyisourate hydrolase, 
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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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme is not affected by 1 mM of Cr3+, Mg2+, or Ca2+
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
additional information
addition of 3His to the N-terminal end weakens 5-hydroxyisourate hydrolysis activity, whereas it enhanced T3-binding activity of R54E/Y119T mutsant enzyme
-
additional information
addition of 3His to the N-terminal end weakens 5-hydroxyisourate hydrolysis activity, whereas it enhanced T3-binding activity of R54E/Y119T mutsant enzyme
-
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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
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
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
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
evolution
evolution of transthyretin from 5-hydroxyisourate hydrolase to triiodothyronine distributor to thyroxine distributor
evolution
sequential molecular events of functional trade-offs in 5-hydroxyisourate hydrolase before and after gene duplication led to the evolution of transthyretin during chordate diversification
evolution
sequential molecular events of functional trade-offs in 5-hydroxyisourate hydrolase before and after gene duplication led to the evolution of transthyretin during chordate diversification
metabolism
the enzyme catalyzes the hydrolysis of 5-hydroxyisourate in the purine degradation pathway, and transthyretin, a thyroid hormone binding protein
metabolism
the enzymes is involved in uric acid metabolism
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
R54E/Y119T
amino acid substitutions, R54E/Y119T, at the active sites of HIUHase, exert weak [125I]-3,3',5-triiodo-l-thyronine([125I]T3) binding activity with a concomitant loss of 5-hydroxyisourate hydrolysis activity
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
R54E/Y119T
amino acid substitutions, R54E/Y119T, at the active sites of HIUHase, exert weak [125I]-3,3',5-triiodo-l-thyronine([125I]T3) binding activity with a concomitant loss of 5-hydroxyisourate hydrolysis activity
additional information
E199A
site-directed mutagenesis, mutant devoid of detectable catalytic activity
E408A
site-directed mutagenesis, mutant devoid of detectable catalytic activity
additional information
the deletion mutation DELTAYRGS greatly affects activity
additional information
-
the deletion mutation DELTAYRGS greatly affects 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 enzyme
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 Rosetta 2(DE3)pLysS
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 (O32142), Bacillus subtilis
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 (Q06S87), Danio rerio
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 (Q9CRB3), Mus musculus
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 (P76341), Escherichia coli, 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 (U6C7K1), Oncorhynchus mykiss
brenda
Richardson, S.
Tweaking the structure to radically change the function The evolution of transthyretin from 5-hydroxyisourate hydrolase to triiodothyronine distributor to thyroxine distributor
Front. Endocrinol. (Lausanne)
5
245
2015
Salmonella enterica subsp. enterica serovar Dublin (Q4VYA5)
brenda
Yamauchi, K.; Kasai, K.
Sequential molecular events of functional trade-offs in 5-hydroxyisourate hydrolase before and after gene duplication led to the evolution of transthyretin during chordate diversification
J. Mol. Evol.
86
457-469
2018
Oncorhynchus mykiss (K9MS40), Branchiostoma japonicum (K9MS40)
brenda
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