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RISS 인기검색어
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- 저자 : 김유삼 ( Hye Sin Byun (검색결과 2 건)
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변혜신,김유삼,Byun, Hye-Sin,Kim, Yu-Sam 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.4
단백질에서 arginine에 특이적으로 반응하는 2,3-butanedione과 phenylglyoxal을 Saccharomyes cereνisiae glucose-6-phosphate dehydrogenase의 촉매반응에 관여하는 아미노산을 밝히는데 사용하였다. 2,3-Butanedione은 biphasic mode로 즉 초기에는 빠르게 그리고 나서는 느리게 이 효소를 불활성화시켰다. 이 초기단계에서의 2차 반응속도상수는 $344.8M^{-1}min^{-1}$이었고 반응차수가 0.87인 것으로 보아서 효소분자당 한 분자의 2,3-butanedione이 작용하는 것으로 판단된다. 또 효소를 $NADP^+$와 처리하였을 때 이러한 불활성화반응이 보호되며, 이것은 효소의 활성에 중요하게 관여하는 하나의 arginine이 $NADP^+$ 결합부위에 존재한다는 것을 제시하는 것이다. 이 효소는 phenylglyoxal에 의해서도 불활성화 되며 이에 대한 2차 반응속도상수는$185.7M^{-1}min^{-1}$이고 반응차수는 0.90으로 2,3-butanedione에 의해서 얻은 결과들을 더욱 뒷받침한다. Arginine specific reagents, 2,3-butanedione and phenylglyoxal, were used to determine amino acid residues essential for glucose-6-phosphate dehydrogenase catalysis of Saccharomyces cerevisiae. 2,3-Butanedione inactivated the enzyme in biphasic mode, initially rapid and then slow. The second-order rate constant for the initial-phase inactivation in 10 mM sodium borate buffer, pH 8.8, at $30^{\circ}C$ was calculated to be $344.8M^{-1}min^{-1}$. The order of the inactivation with respect to 2,3-butanedione was 0.87, indicating that one molecule of the reagent rapidly bind to one active unit of the enzyme. The inactivation by 2,3-butanedione was protected by a preincubation of the enzyme with $NADP^+$, suggesting that the essential arginine for the enzyme activity may be located at or near the binding region of $NADP^+$. Phenylglyoxal also rapidly inactivated the enzyme with the second-order rate constant of inactivation, $185.7M^{-1}min^{-1}$ and with the reaction order of 0.90, supporting the experimental result with 2,3-butanedione.
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효모 glucose - 6 - phosphate dehydrogenase 의 NADP + 결합부위에 있는 arginine
변혜신,김유삼 ( Hye Sin Byun,Yu Sam Kim ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.4
Arginine specific reagents, 2,3-butanedione and phenylglyoxal, were used to determine amino acid residues essential for glucose-6-phosphate dehydrogenase catalysis of Saccharomyces cerevisiae. 2,3-Butanedione inactivated the enzyme in biphasic mode, initially rapid and then slow. The second-order rate constant for the initial-phase inactivation in 10 mM sodium borate buffer, pH 8.8, at 30℃ was calculated to be 344.8 M^(-1)min^(-1). The order of the inactivation with respect to 2,3-butanedione was 0.87, indicating that one molecule of the reagent rapidly bind to one active unit of the enzyme. The inactivation by 2,3-butanedione was protected by a preincubation of the enzyme with NADP^+, suggesting that the essential arginine for the enzyme activity may be located at or near the binding region of NADP^+. Phenylglyoxal also rapidly inactivated the enzyme with the second-order rate constant of inactivation, 185.7 M^(-1)min^(-1) and with the reaction order of 0.90, supporting the experimental result with 2,3-butanedione.
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