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Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction

Authors
Lee, YLee, DHKho, CWLee, AYJang, MCho, SLee, CHLee, JSMyung, PKPark, BCPark, SG
Issue Date
29-Aug-2005
Publisher
ELSEVIER SCIENCE BV
Keywords
uric acid; uricase; hydroxyisourate; PucM; transthyretin-related proteins
Citation
FEBS LETTERS, v.579, no.21, pp 4769 - 4774
Pages
6
Journal Title
FEBS LETTERS
Volume
579
Number
21
Start Page
4769
End Page
4774
URI
https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24543
DOI
10.1016/j.febslet.2005.07.056
ISSN
0014-5793
Abstract
Purine catabolic pathway in Bacillus subtilis is consisted of more than 14 genes. Among these genes, pucL and pucM are required for uricase activity. While PucL is known to encode the uricase itself, the function of PucM is still unclear although this protein is also indispensable for uric acid decomposition. Here, we provide evidence that PucM, a transthyretin-related protein, functions to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction. Based on these results, we propose that transthyretin-related proteins present in diverse organisms are not functionally related to transthyretin but actually function as a hydroxyisoorate hydrolase. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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