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RISS 인기검색어
- 검색키워드
- 저자 : 강승우 ( Yu Sam Kim (검색결과 2 건)
- 무료
- 기관 내 무료
- 유료
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Isolation of a Novel Malonate Kinase from Acinetobacter calcoaceticus Grown on Malonate
김유삼,김성준,이종서,강승우,Kim, Yu-Sam,Kim, Seong-Jun,Lee, Jong-Seo,Kang, Seung-Woo Korean Society for Biochemistry and Molecular Biol 1991 한국생화학회지 Vol.24 No.1
Malonate kinase is a novel enzyme that catalyzed the formation of malonylphosphate directly from malonate and ATP. The enzyme was induced in malonate-grown Acinetobacter caloaceticus and activated by sulfate ion and by Triton X-100. The enzyme was purified by a combination of ammonium sulfate precipitation, Affi-gel blue, polybuffer exchanger 94, $\omega$-aminohexyl agarose, and hydroxyapatite chromatography. The enzyme was composed of two proteins, protein A and protein B, separated on polybuffer exchanger 94. The protein A was 63,000 dalton monomer and the protein B was 96,000 dalton dimer ($2{\times}48,000$). This enzyme showed a high substrate specificity on malonate and ATP, and required $Mg^{2+}$ or $Mn^{2+}$. Optimal pH was 7.2. Malonate kinase는 malonate와 ATP로부터 직접적으로 malonylphosphate를 만드는 반응에 작용하는 새로운 효소이다. 이 효소는 malonate 배지에서 자란 Acinetobacter calcoaceticus에서 유도되며 sulfate ion과 Triton X-100에 의하여 활성이 증가된다. 이 효소를 ammonium sulfate precipition, Affi-gel bule, poly buffer exchanger 94, $\omega$-aminohexyl agarose와 hydroxyapatite chromatography에 의하여 정제하였다. 이 효소는 poly buffer exchanger 94에서 분리되는 단백질 A와 단백질 B로 구성되어 있다. 단백질 A는 63,000 dalton의 monomer이고 단백질 B는 96,000 dalton인데 이것은 48,000 dalton 단백질 둘로 되어 있다. 이것은 malonate와 ATP에 대하여 높은 기질 특이성을 나타냈다. 또 이 효소는 $Mg^{2+}$ 또는 $Mn^{2+}$을 요구하며, 최적 pH는 7.2였다.
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말론산배지에 자란 Acinetobacter calcoaceticus 에서 새로운 Malonate Kinase 의 분리
김유삼,김성준,이종서,강승우 ( Yu Sam Kim,Seong Jun Kim,Jong Seo Lee,Seung Woo Kang ) 생화학분자생물학회 1991 BMB Reports Vol.24 No.1
Malonate kinase is a novel enzyme that catalyzed the formation of malonylphosphate directly from malonate and ATP. The enzyme was induced in malonate-grown Acinetobacter caloaceticus and activated by sulfate ion and by Triton X-100. The enzyme was purified by a combination of ammonium sulfate precipitation, Affi-gel blue, polybuffer exchanger 94, ω-aminohexyl agarose, and hydroxyapatite chromatography. The enzyme was composed of two proteins, protein A and protein B, separated on polybuffer exchanger 94. The protein A was 63,000 dalton monomer and the protein B was 96,000 dalton dimer (2×48,000). This enzyme showed a high substrate specificity on malonate and ATP, and required Mg^(2+) or Mn^(2+). Optimal pH was 7.2.
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