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RISS 인기검색어
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- 저자 : 김유삼 ( Son Kwon Bang (검색결과 2 건)
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Chemical Modification of Pseudomonas fluorescens Malonyl-CoA Synthetase with Pyridoxal-5'-Phosphate
방선권,김유삼,Bang, Son-Kwon,Kim, Yu-Sam 생화학분자생물학회 1990 한국생화학회지 Vol.23 No.2
Pseudomonas fluorescens에서 정제한 malonyl-CoA synthetase는 pyridoxal-5'-phosphate에 의해서 비가역적으로 불활성화되었다. 불활성화 과정은 biphasic이었으며 처음 phase에서의 2차 반응속도는 $30^{\circ}C$, pH 7.0에서 $175M^{-1}min^{-1}$이었다. 다음 phase의 불활성화에서는 325nm에서의 흡광과 392nm에서의 형광을 동반하였다. 이런 현상은 $NaBH_4$의 환원을 시켰을 때와 시키지 않았을 때 동일하였으며 이것은 다음 phase를 지나서는 X-azolidine과 유사한 complex가 형성되는 것을 의미한다. Malonate는 pyridoxal 5'-phosphate의 불활성화를 막았으며 malony-CoA synthetase의 두 subunit 들 중에서 ${\alpha}$-subunit에 이러한 불활성화에 관련된 group이 존재하였다. 이러한 결과들은 malonyl-CoA synthetase ${\alpha}$-subunit의 malonate binding site에 효소활성에 필수적인 amino group이 존재한다는 것을 뜻한다. Malonyl-CoA synthetase from Pseudomonas fluorescens was irreversibly inactivated by pyridoxal-5'-phosphate. The course of inactivation appeared to be biphasic. The second-order rate constant, $K_2$, for the first phase of inactivation was $175M^{-1}{\cdot}min^-1$ at pH 7.0 and $30^{\circ}C$. The inactivation at second phase was accompanied by a new absorbance at 325 nm and a fluorescence emission at 392 nm without $NaBH_4$ reduction, suggesting the formation of X-azolidine-like complex. The incubation of the enzyme with malonate prior to pyridoxal-5'-phosphate treatment protected the inactivation. When alpha subunit but not beta subunit of the enzyme was treated with pyridoxal-5'-phosphate, the enzyme was inactivated, indicating that an essential amine is located at or near the malonate binding site of alpha subunit of the enzyme.
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Pyridoxal - 5 ' - phosphate 에 의한 Pseudomonas fluorescens malonyl - CoA synthetase 의 화학 변형
방선권,김유삼 ( Son Kwon Bang,Yu Sam Kim ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.2
Malonyl-CoA synthetase from Pseudomonas fluorescens was irreversibly inactivated by pyridoxal-5`-phosphate. The course of inactivation appeared to be biphasic. The second-order rate constant, k₂, for the first phase of inactivation was 175 M^(-1)·min^(-1) at pH 7.0 and 30℃. The inactivation at second phase was accompanied by a new absorbance at 325 nm and a fluorescence emission at 392 nm without NaBH₄ reduction, suggesting the formation of X-azolidine-like complex. The incubation of the enzyme with malonate prior to pyridoxal-5`-phosphate treatment protected the inactivation. When alpha subunit but not beta subunit of the enzyme was treated with pyridoxal-5`-phosphate, the enzyme was inactivated, indicating that an essential amine is located at or near the malonate binding site of alpha subunit of the enzyme.
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