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학술발표회초록보기

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  • 08월 18일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제108회 대한화학회 학술발표회, 총회 및 기기전시회 안내 FrsA functions as a cofactor-independent decarboxylase to control metabolic flux

등록일
2011년 8월 2일 17시 48분 47초
접수번호
1420
발표코드
BIO2-4 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 11시 : 00분
발표형식
심포지엄
발표분야
생명화학 - Structural Biochemistry and Cellular Signaling
저자 및
공동저자
차선신
한국해양연구원 해양바이오연구센터, Korea
Bacteria develops the phosphoenolpyruvate (PEP):sugar phosphotransferase system (PTS) whose components participate in a variety of regulatory processes. Glucose-specific enzyme IIAGlc, a component of PTS, interacts with several target proteins, regulating their activity. Fermentation/respiration switch (FrsA) protein, one of IIAGlc-binding proteins, is known to increase glucose fermentation under oxygen-limited conditions. Here, we demonstrate that FrsA is a proficient enzyme that converts pyruvate to acetaldehyde and carbon dioxide in a cofactor-independent manner, which contrasts with the established notion that the decarboxylation of alpha-keto acids depends on a cofactor. According to the crystal structures, FrsA assumes the canonical alpha/beta hydrolase structure but contains no catalytic machinery for hydrolytic reactions. Structure-based identification of three amino acids (Arg53, Asp203, and Arg272) critical for pyruvate decarboxylation, together with no requirement of cofactors in catalysis, leads us to propose a direct decarboxylation mechanism that is based on electrostatic repulsion. Furthermore, we show that IIAGlc enhances the enzymatic activity of FrsA by modulating the active site conformation, revealing the biological implication of complex formation between FrsA and IIAGlc.

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