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Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.2.17 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

EC Number Protein Variants Comment Organism
3.5.2.17 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
3.5.2.17 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
3.5.2.17 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

EC Number Organism UniProt Comment Textmining
3.5.2.17 Danio rerio Q06S87
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-

Synonyms

EC Number Synonyms Comment Organism
3.5.2.17 HIUase
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Danio rerio