Mouse Transthyretin-related Protein Is a Hydrolase which Degrades 5-Hydroxyisourate, the End Product of the Uricase Reaction
2006
Lee, Y.R. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea) | Park, B.C. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea) | Lee, D.H. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea) | Bae, K.H. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea) | Cho, S.Y. (Chung-Ang University, Seoul, Republic of Korea) | Lee, C.H. (Konkuk University, Seoul, Republic of Korea) | Lee, J.S. (Konkuk University, Seoul, Republic of Korea) | Myung, P.K. (Chungnam National University, Daejeon, Republic of Korea) | Park, S.G. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), E-mail: sgpark@kribb.re.kr
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.
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