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Title 

Structural and functional analysis of PucM, a hydrolase in the ureide pathway and a member of the transthyretin-related protein family

 

PucM 구조 분석

Authors 

D K JungYou Ra LeeSung Goo ParkByoung Chul ParkG H KimS Rhee

Publisher 

National Academy of Sciences

Issue Date 

2006

Citation 

Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 26, pp. 9790-9795

Keywords 

5-hydroxyisourate hydrolasebacillus subtilispurine catabolism5 hydroxyisourate5,6 diaminouracil8 azaxanthineamino acidargininehydrolaseprealbumin

Abstract 

The ureide pathway, which produces ureides from uric acid, is an essential purine catabolic process for storing and transporting the nitrogen fixed in leguminous plants and some bacteria. PucM from Bacillus subtilis was recently characterized and found to catalyze the second reaction of the pathway, hydrolyzing 5-hydroxyisourate (HIU), a product of uricase in the first step. PucM has 121 amino acid residues and shows high sequence similarity to the functionally unrelated protein transthyretin (TTR), a thyroid hormone-binding protein. Therefore, PucM belongs to the TTR-related proteins (TRP) family. The crystal structures of PucM at 2.0 ? and its complexes with the substrate analogs 8-azaxanthine and 5,6-diaminouracil reveal that even with their overall structure similarity, homotetrameric PucM and TTR are completely different, both in their electrostatic potential and in the size of the active sites located at the dimeric interface. Nevertheless, the absolutely conserved residues across the TRP family, including His-14, Arg-49, His-105, and the C-terminal Tyr-118-Arg-119-Gly-120-Ser-121, indeed form the active site of PucM. Based on the results of site-directed mutagenesis of these residues, we propose a possible mechanism for HIU hydrolysis. The PucM structure determined for the TRP family leads to the conclusion that diverse members of the TRP family would function similarly to PucM as HIU hydrolase.

ISSN 

0027-8424

Link 

http://dx.doi.org/10.1073/pnas.0600523103

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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