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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

Reaction

5-hydroxyisourate
+
H2O
=
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate

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 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.2 In cyclic amides
                3.5.2.17 hydroxyisourate hydrolase

Engineering

Engineering on EC 3.5.2.17 - hydroxyisourate hydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
E199A
E408A
H101A
-
10% of wild-type activity
H7A
-
3% of wild-type activity
Y114F
-
22% of wild-type activity
H7N
dramatic decrease in activity
H92N
dramatic decrease in activity
R41K
about 90% decrease in activity
S108A
about 50% decrease in activity
H7N
-
dramatic decrease in activity
-
H92N
-
dramatic decrease in activity
-
R41K
-
about 90% decrease in activity
-
S108A
-
about 50% decrease in activity
-
H102N
10fold reduced activity
H11N
mutant almost abolishes activity
R51E
mutant almost abolishes activity
R51K
mutant fails to affect activity
S118A
mutation has no influence on activity
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