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Structural Basis of 5-Hydroxyisourate Hydrolysis by PucM

등록일
2006년 8월 30일 15시 01분 39초
접수번호
1276
발표코드
금14A5심 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 11시 : 30분
발표형식
심포지엄
발표분야
생명화학 - Enzyme Catalysis and Regulation
저자 및
공동저자
이상기
서울대학교 농생명공학부,
The ureide pathway is an essential purine catabolic process in leguminous plants, as well as some bacteria. PucM from Bacillus subtilis was recently found to hydrolyze 5-hydroxyisourate in the pathway. It shows high sequence similarity to the functionally unrelated protein transthyretin, therefore, belonging to the transthyretin-related proteins (TRP) family. The crystal structures of PucM and its complexes with the substrate analogs reveal that even with their overall structure similarity, homotetrameric PucM and transthyretin 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 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.

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