Mouse transthyretin-related protein is a hydrolase which degrades 5-Hydroxyisourate, the end product of the uricase reaction

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dc.contributor.authorYou Ra Lee-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorDo Hee Lee-
dc.contributor.authorKwang-Hee Bae-
dc.contributor.authorS Cho-
dc.contributor.authorC H Lee-
dc.contributor.authorJong Suk Lee-
dc.contributor.authorP K Myung-
dc.contributor.authorSung Goo Park-
dc.date.accessioned2017-04-19T09:05:24Z-
dc.date.available2017-04-19T09:05:24Z-
dc.date.issued2006-
dc.identifier.issn1016-8478-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7626-
dc.description.abstractUric 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 Cterminal 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.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleMouse transthyretin-related protein is a hydrolase which degrades 5-Hydroxyisourate, the end product of the uricase reaction-
dc.title.alternativeMouse transthyretin-related protein is a hydrolase which degrades 5-Hydroxyisourate, the end product of the uricase reaction-
dc.typeArticle-
dc.citation.titleMolecules and Cells-
dc.citation.number2-
dc.citation.endPage145-
dc.citation.startPage141-
dc.citation.volume22-
dc.contributor.affiliatedAuthorYou Ra Lee-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorDo Hee Lee-
dc.contributor.affiliatedAuthorKwang-Hee Bae-
dc.contributor.affiliatedAuthorJong Suk Lee-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.alternativeName이유라-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName이도희-
dc.contributor.alternativeName배광희-
dc.contributor.alternativeName조사연-
dc.contributor.alternativeName이충환-
dc.contributor.alternativeName이종석-
dc.contributor.alternativeName명평근-
dc.contributor.alternativeName박성구-
dc.identifier.bibliographicCitationMolecules and Cells, vol. 22, no. 2, pp. 141-145-
dc.subject.keywordhydroxyisourate-
dc.subject.keywordtransthyretin-related proteins-
dc.subject.keyworduric acid-
dc.subject.keyworduricase-
dc.subject.localhydroxyisourate-
dc.subject.localtransthyretin-related proteins-
dc.subject.localuric acid-
dc.subject.localuricase-
dc.description.journalClassY-
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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