Purification and Characterization of N-Acetylneuraminate Synthase from Escherichia coli K1-M12
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概要
- 論文の詳細を見る
N-Acetylneuraminate (NeuAc) synthase, which catalyzes NeuAc synthesis by condensation of N-acetyl-D-mannosamine (ManNAc) and phosphoenolpyruvate (PEP), was purified from a cell extract of Escherichia coli K1-M12 to electrophoretically homogeneity by serial column chromatographies. The molecular weight of native enzyme was estimated to be 106,000 by gel filtration. After denaturation in sodium dodecyl sulfate, the molecular weight was reduced to 52,000, indicating the existence of 2 identical subunits. The optimum pH was 7.5 and the stable pH range was 7.0 to 10.0. The enzyme was thermostable up to 30℃. No metal ion was required for the enzyme activity. SH-inhibitors such as p-chloromercuribenzoic acid and mercury chloride were potent inhibitors. The K_m for ManNAc and PEP were 5.6 mM and 0.04 mM, respectively.
- 社団法人日本農芸化学会の論文
- 1997-12-23
著者
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OHTA Yasuhiro
Kyoto Research Laboratories, Marukin Shoyu Co. Ltd.
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太田 泰広
神戸大学自然科学研究科
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太田 泰広
広島大学工学部
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Ohta Y
Marukin Bio Inc.
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TSUKADA Yoji
Kyoto Research Laboratories, Marukin Shoyu Co., Ltd.
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Tsukada Y
Marukin Bio Inc.
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Tsukada Yoji
Kyoto Research Laboratories Marukin Shoyu Co. Ltd.
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KOMAKI Eriko
Marukin Bio, Inc.
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KOMAKI Eriko
Kyoto Research Laboratories, Marukin Shoyu Co., Ltd.
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Komaki Eriko
Marukin Bio Inc.
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Ohta Yasuhiro
Kyoto Research Laboratories Marukin Shoyu Co. Ltd
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OHTA Yasuhiro
Department of Applied Physics, Faculty of Engineering University of Tokyo
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