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Vertebrate 5-Hydroxyisourate Hydrolase Identification, Function, Structure, and Evolutionary Relationship with Transthyretin

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Recent Advances in Transthyretin Evolution, Structure and Biological Functions

Abstract

5-Hydroxyisourate hydrolase (HIUase) is an enzyme widely distributed in prokaryotic and eukaryotic organisms that catalyzes the hydrolysis of HIU into OHCU in the degradation route from urate to (S)-allantoin. During early vertebrate evolution, a duplication event in the gene encoding HIUase gave rise to the thyroid hormone binding protein transthyretin (TTR). Due to the close evolutionary relationship between HIUase and TTR, these two proteins possess a high degree of amino acid sequence similarity, while performing quite different functions. The 3D structure of zebrafish HIUase compares very well with that of TTR: a highly preserved scaffold harbors distinct functional sites located in the same regions of the two proteins. The residues that are differentially conserved in HIUase as compared to TTR map in catalytic regions occupying the outer portions of the two halves of the central channel that transverses the whole tetrameric proteins. The evolution of HIUase into TTR has been accompanied by remarkable changes of the catalytic sites to give rise to a channel open at both ends, thus allowing free access to hormone molecules.

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Author information

Authors and Affiliations

  1. Department of Biological Chemistry, University of Padua, and ICB-CNR, Section of Padua, Viale G. Colombo 3, 35121, Padova, Italy

    Giuseppe Zanotti

  2. Department of Biochemistry and Molecular Biology, University of Parma, Viale delle Scienze 23/A, 43100, Parma, Italy

    Ileana Ramazzina, Claudia Folli, Riccardo Percudani & Rodolfo Berni

  3. Department of Chemistry, University of Padua, and ICB-CNR, Section of Padua, Via Marzolo 1, 35131, Padova, Italy

    Laura Cendron

  4. Venetian Institute of Molecular Medicine, Via Orus 2, 35127, Padua, Italy

    Laura Cendron

Authors
  1. Giuseppe Zanotti
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  2. Ileana Ramazzina
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  3. Laura Cendron
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  4. Claudia Folli
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  5. Riccardo Percudani
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  6. Rodolfo Berni
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Corresponding author

Correspondence to Giuseppe Zanotti .

Editor information

Editors and Affiliations

  1. School of Medical Sciences, RMIT University, Bundoora, VIC 3083, Bundoora West Campus, Australia

    Samantha J. Richardson

  2. Medical Research Institute, Hauptman-Woodward, 700 Elliott Street, Buffalo, NY, 14203, USA

    Vivian Cody

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© 2009 Springer-Verlag Berlin Heidelberg

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Zanotti, G., Ramazzina, I., Cendron, L., Folli, C., Percudani, R., Berni, R. (2009). Vertebrate 5-Hydroxyisourate Hydrolase Identification, Function, Structure, and Evolutionary Relationship with Transthyretin. In: Richardson, S.J., Cody, V. (eds) Recent Advances in Transthyretin Evolution, Structure and Biological Functions. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-00646-3_6

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