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Information on EC 3.5.2.17 - hydroxyisourate hydrolase and Organism(s) Danio rerio and UniProt Accession Q06S87

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IUBMB 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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This record set is specific for:
Danio rerio
UNIPROT: Q06S87
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Word Map
The taxonomic range for the selected organisms is: Danio rerio
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
transthyretin, transthyretin-like protein, hydroxyisourate hydrolase, hiuhase, 5-hydroxyisourate hydrolase, transthyretin-related protein, hiu hydrolase, hiuase, sbttr, ectrp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-hydroxyisourate hydrolase
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5-hydroxyisourate hydrolase
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HIUHase
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-
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
255885-20-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-hydroxyisourate + H2O
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HIUH_DANRE
138
0
15486
Swiss-Prot
other Location (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
x-ray crystallography
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D50N
shows 50% activity of the wild type enzyme
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team