Carbamoyl Phosphate Synthetase of the Cyanobacterium Anabaena cylindrica
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概要
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Carbamoyl phosphate synthetase from the cyanobacte-rium Anabaena cylindrica was purified by the following procedures: ammoniun sulfate fractionation, DEAE-Toyo-pearl, Affi-gel Blue. Sephacryl S-300 HR, and Mono Q column chromatography. The molecular weight of the holoenzyme was estimated to be 166,000 by gel permeation chromatography. SDS-PAGE showed that the enzyme consisted of two subunits with molecular weights of 130,000 and 43,000. Optimal pH of this enzyme was 7.8 in HEPES buffer. Its MgATP saturation curve was sigmoidal, yielding a Hill coefficient of 1.9 and an apparent K_m of 4.5 mM. The K_m values for glutamine, NH_4Cl and NaHCO_3 Were 55 μM, 182 mM and 2.5 mM, respectively. A high concentration of K^+ (100 mM) was required for maximum activity. The enzyme was activated by ornithine, IMP, GMP, and GDP, and inhibited by UMP and UDP. Ornithine increased the affinity of the enzyme to ATP by acting as a positive allosteric effector, whereas UMP reduced it by acting as a negative allosteric effector.
- 日本植物生理学会の論文
著者
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Ohmori Masayuki
Department Of Life Sciences Graduate School Of Arts And Sciences The University Of Tokyo
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Kasahara Masahiro
Department Of Computational Biology Graduate School Of Frontier Science University Of Tokyo
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Kasahara Masahiro
Department Of Life Sciences Graduate School Of Arts And Sciences The University Of Tokyo
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Ohmori Masayuki
Department Of Biological Sciences Faculty Of Science And Engineering Chuo University
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Ohmori Masayuki
Department Of Biochemistry And Molecular Biology Faculty Of Science Saitama University
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KASAHARA Masahiro
Department of Biotechnology, College of Life Sciences, Ritsumeikan University
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Ohmori Masayuki
Department of Life Sciences, Graduate School of Arts and Sciences,The University of Tokyo
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