Literature summary for 3.5.2.17 extracted from

Cendron, L.; Ramazzina, I.; Percudani, R.; Rasore, C.; Zanotti, G.; Berni, R.
Probing the evolution of hydroxyisourate hydrolase into transthyretin through active-site redesign (2011), J. Mol. Biol., 409, 504-512.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Danio rerio

Crystallization (Comment)

Organism

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

Danio rerio

Protein Variants

Protein Variants	Comment	Organism
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	Danio rerio
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	Danio rerio
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	Danio rerio

Organism

Organism	UniProt	Comment	Textmining
Danio rerio	Q06S87	-	-

Synonyms

Synonyms	Comment	Organism
HIUase	-	Danio rerio