Purification and Properties of Phthalate Oxygenase from Rhodococcus erythropolis S-1
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概要
- 論文の詳細を見る
Phthalate oxygenase was induced in Rhodococcus erythropolis S-1, a Gram-positive bacterium, when this bacterium was cultured in a medium containing phthalate as a sole carbon source. The enzyme was purified 118-fold with 4.7% activity yield. The purified enzyme appeared homogenous on native PAGE. This enzyme is a large protein (213 kDa), a tetramer of identical 56 kDa monomers, and a flavoprotein Containing FAD with NADH-dependent dioxygenase activity. The enzyme is specific for phthalate and other closely related aromatic compounds. Optimum pH and temperature were 6.5 and 40℃. The K_m for phthalate and NADH were 0.040 mM and 0.069 mM. The enzyme catalyzes dihydroxylation of phthalate to form 3, 4-dihydro-3, 4-dihydroxyphthalate with consumption of NADH and oxygen.
- 社団法人日本農芸化学会の論文
- 1993-09-23
著者
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Suemori A
National Inst. Biosci. And Human‐technol. (nibh) Ibaraki Jpn
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Suemori Akio
National Institute Of Bioscience And Human-technology (nibh)
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KURANE Ryuichiro
National Institute of Bioscience and Human-Technology (NIBH)
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TOMIZUKA NOBORU
Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
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Tomizuka Noboru
National Institute of Bioscience and Human-Technology (NIBH)
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Tomizuka Noboru
National Institute Of Bioscience And Human-technology
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Kurane R
National Inst. Advanced Industrial Sci. And Technol. Tsukuba Jpn
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Kurane Ryuichiro
National Institute Of Biosciecne And Human Technology Agency Of Industrial Science And Technology Ministry Of International Trade & Industry
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