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Acinetobacter calcoaceticus 인산아세탈기 전달효소의 Acetylphosphate 결합부위에 있는 Thiol 및 amine group
고정헌,김유삼 ( Jeong Heon Ko,Yu Sam Kim ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.2
Phosphate acetyltransferase from Acinetobacter calcoaceticus grown on malonate as a sole source of carbon is inhibited by thiol group directed reagents, 5,5`-dithio-bis(2-nitrobenzoic acid) and p-chloromercuriphenylsulfonic acid, and by amino group directed reagents, pyridoxal-5`-phosphate and o-phthalaldehyde, respectively. The second-order rate constants of the inactivation by 5,5`-dithio-bis(2-nitrobenzoic acid) and pyridoxal-5`-phosphate were 21 M^(-1) min^(-1) and 483 M^(-1) min^(-1), respectively. The inactivation by the reagents is protected by acetylphosphate, indicating that thiol and amino groups essential for the enzyme activity are located on the acetylphosphate binding region of the active site.
고정헌,김유삼,Ko, Jeong-Heon,Kim, Yu-Sam 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.2
말론산을 유일한 탄소원으로 하여 생육한 Acinetobacler calcoaceticus의 인산아세틸기 전달효소는 5, 5'-dithio-bis(2-nitrobenzoic acid), p-chloromercusiphenylsulfonic acid, pyridoxal-5'-phosphate, o-phthalaldehyde 에 의해서 각각 그 활성이 억제되었다. 5, 5'-dithio-bis(2-nitrobenzoic acid)와 pyridoxal-5'-phosphate에 의한 비활성화의 2차 반응속도 상수는 $21M^{-1}min^{-1}$와 $483M^{-1}min^{-1}$이었다. 또 이들에 의한 비활성화는 acetylphosphate에 의해서 보호되는 것으로 미루어 디올기와 아민기가 활성자리의 acetylphosphate 결합부위에 존재함을 예측하게 한다. Phosphate acetyltransferase from Acinetobacter calcoaceticus grown on malonate as a sole source of carbon is inhibited by thiol group directed reagents, 5,5'-dithio-bis(2-nitrobenzoic acid) and p-chloromercuriphenylsulfonic acid, and by amino group directed reagents, pyridoxal-5'-phosphate and o-phthalaldehyde, respectively. The second-order rate constants of the inactivation by 5,5'-dithio-bis(2-nitrobenzoic acid) and pyridoxal-5'-phosphate were 21 $M^{-1}$ $min^{-1}$ and 483 $M^{-1}$ $min^{-1}$, respectively. The inactivation by the reagents is protected by acetylphosphate, indicating that thiol and amino groups essential for the enzyme activity are located on the acetylphosphate binding region of the active site.