Molecules and Cells

  • 제22권2호
  • /
  • Pages.141-145
  • /
  • 2006
  • /
  • 1016-8478(pISSN)
  • /
  • 0219-1032(eISSN)
한국분자세포생물학회 (Korean Society for Molecular and Cellular Biology)
권호 표지

Mouse Transthyretin-related Protein Is a Hydrolase which Degrades 5-Hydroxyisourate, the End Product of the Uricase Reaction

  • Lee, Youra (Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Park, Byoung Chul (Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Lee, Do Hee (Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Bae, Kwang-Hee (Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Cho, Sayeon (College of Pharmacy, Chung-Ang University) ;
  • Lee, Choong Hwan (Division of Bioscience and Biotechnology, IBST, Konkuk University) ;
  • Lee, Jong Suk (Division of Bioscience and Biotechnology, IBST, Konkuk University) ;
  • Myung, Pyung Keun (College of Pharmacy, Chungnam National University) ;
  • Park, Sung Goo (Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
  • 투고 : 2005.10.11
  • 심사 : 2006.05.23
  • 발행 : 2006.10.31
⟨ 이전 논문 다음 논문 ⟩

초록

Uric acid is the end product of the purine degradation pathway in humans. It is catabolized to allantoin by urate oxidase or uricase (E.C. 1.7.3.3.) in most vertebrates except humans, some primates, birds, and certain species of reptiles. Here we provide evidence that mouse transthyretin-related protein facilitates the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction. Mutagenesis experiments showed that the residues that are absolutely conserved across the TRP family, including His11, Arg51, His102, and the C-terminal Tyr-Arg-Gly-Ser, may constitute the active site of mTRP. Based on these results, we propose that the transthyretin-related proteins present in diverse organisms are not functionally related to transthyretin but actually function as hydroxyisourate hydrolases.

키워드

과제정보

연구 과제 주관 기관 : Ministry of Science and Technology, Ministry of Industry, Commerce and Energy of Korea

참고문헌

  1. Bongaerts, G. P. A., Uitzetter, J., Brouns, R., and Vogels, G. D. (1978) Uricase of Bacillus fastidiosus: properties and regulation of synthesis. Biochem. Biophys. Acta 527, 348-358 https://doi.org/10.1016/0005-2744(78)90349-2
  2. Eneqvist, T., Lundberg, E., Nilsson, L., Abagyan, R., and Sauer- Eriksson, A. E. (2003) The transthyretin-related protein family. Eur. J. Biochem. 270, 518-532 https://doi.org/10.1046/j.1432-1033.2003.03408.x
  3. Kahn, K. and Tipton, P. A. (1997) Kinetic mechanism and cofactor content of soybean root noodle urate oxidase. Biochemistry 36, 4731-4738 https://doi.org/10.1021/bi963184w
  4. Kahn, K. and Tipton, P. A. (1998) Spectroscopic characterization of intermediates in the urate oxidase reaction. Biochemistry 37, 11651-11659 https://doi.org/10.1021/bi980446g
  5. Kahn, K., Serfozo, P., and Tipton, P. A. (1997) Identification of the true product of the urate oxidase reaction. J. Am. Chem. Soc. 119, 5435-5224 https://doi.org/10.1021/ja970375t
  6. Keilin, J. (1959) Biological significance of uric acid on guanine excretion. Biol. Rev. 34, 265-296
  7. Lee, K. W. and Roush, A. H. (1964) Allantoinase assays and their application to yeast and soybean allantoinases. Arch. Biochem. Biophys. 108, 460-467 https://doi.org/10.1016/0003-9861(64)90427-8
  8. Lee, H., Hur, C.-G., Oh, C. J., Kim, H. B., Park, S-Y., et al. (2004) Analysis of the root nodule-enhanced transcriptome in soybean. Mol. Cells 18, 53-62
  9. Lee, Y., Lee, D. H., Kho, C. W., Lee, A. Y., Jang, M., et al. (2005) Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction. FEBS Lett. 579, 4769-4774 https://doi.org/10.1016/j.febslet.2005.07.056
  10. Nygaard, P. (1983) Utilization of preformed purine bases and nucleotides; in Metabolism of Nucleotides, Nucleosides and Nucleobases in Microorganisms, Muchch-Petersen, A. (ed.), pp. 27-93, Academic Press, London, UK
  11. Pitts, O. M., Priest, D. G., and Fish, W. W. (1974) Uricase. Subunit composition and resistance to denaturants. Biochemistry 13, 888-892 https://doi.org/10.1021/bi00702a009
  12. Ramazzina, I., Folli, C., Secchi, A., Berni, R., and Percudani, R. (2006) Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes. Nat. Chem. Biol. 2, 144-148 https://doi.org/10.1038/nchembio768
  13. Sarma, A. D., Serfozo, P., Kahn, K., and Tipton, P. A. (1999) Identification and purification of hydroxyisourate hydrolase, a novel ureide-metabolizing enzyme. J. Biol. Chem. 274, 33863-33865 https://doi.org/10.1074/jbc.274.48.33863
  14. Schultz, A. C., Nygaard, P., and Saxild, H. H. (2001) Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator. J. Bacteriol. 183, 3293-3302 https://doi.org/10.1128/JB.183.11.3293-3302.2001
  15. Wu, X., Lee, C. C., Muzny, D. M., and Caskey, C. T. (1989) Urate oxidase: primary structure and evolutionary implications. Proc. Natl. Acad. Sci. USA 86, 9412-9416
  16. Wu, X., Muzny, D. M., Lee, C. C., and Caskey, C. T. (1992) Two independent mutational events in the loss of urate oxidase during hominoid evolution. J. Mol. Evol. 34, 78-84 https://doi.org/10.1007/BF00163854