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Binary Inhibition of Adenine Nucleotides on Phosphotransacetylase from Acinetobacter calcoaceticus
고정헌,김유삼,Ko, Jeong-Heon,Kim, Yu-Sam 생화학분자생물학회 1987 한국생화학회지 Vol.20 No.4
말론산을 유일한 탄소원으로 하여 배양한 Acinetobacter calcoaceticus로 부터 정제한 phosphotransacetylase는 아데닌 뉴클레오티드인 ATP, ADP 그리고 AMP에 의해 그 활성이 방해되었다. 효소를 미리 acetylphosphate와 항온처리하였을 때 ATP는 비 경쟁 방해작용을 나타낸 반면 ADP와 AMP는 무경쟁 방해작용을 보여 주었다. 한편 효소를 coenzyme A와 미리 항온처리한 경우, ATP, ADP는 경쟁적 방해 작용을, AMP는 무경쟁 방해작용을 나타내었다. 이러한 결과들은 ATP와 ADP가 그 억제작용에서 미리 항온처리하는 기질의 조건에 따라 두가지 서로 다른 방향으로 효소 반응을 방해하고 있음을 제시하여 준다. 또한 말론산과 인산도 효소를 coenzyme A와 미리 항온 처리하였을 때 경쟁적 방해 작용을 보여주었다. 이런 일련의 결과들은 ATP와 ADP의 pyrophosphoryl 부분이 기질의 하나인 acetylphosphate와 경쟁적 위치에 있음을 암시해 준다. Phosphotransacetylase, purified from Acinetobacter calcoaceticus grown on malonate as a sole source of carbon, was inhibited by adenine nucleotides, ATP, ADP and AMP. When the enzyme was pre-incubated with acetylphosphate, ATP inhibition was noncompetitive whereas ADP and AMP inhibitions were uncompetitive. However when the enzyme was pre-incubated with coenzyme A, ATP and ADP inhibited competitively whereas AMP did uncompetitively. These results indicated that ATP and ADP inhibited the enzyme in two different ways under the conditions for the pre-incubation with substrates, acetyl phosphate or coenzyme A. In addition to these, malonate and phosphate also inhibited competitively the pre-incubated enzyme with coenzyme A. This result suggests that pyrophosphoryl moiety of ATP and ADP may compete with acetylphosphate.
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.
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.