Partial Purification and Characterization of 4-Hydroxybenzoate-polyprenyltransferase in Ubiquinone Biosynthesis of Pseudomonas putida(Biological Chemistry)
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概要
- 論文の詳細を見る
4-Hydroxybenzoate-polyprenyltransferase, an enzyme in ubiquinone biosynthesis, from Pseudomonas putida was partially purified by ion-exchange and gel filtration column chromatography. The enzyme required phospholipid as and essential factor for actibity. Hexaprenyl pyrophosphate(-PP) and pentaprenyl-PP as well as nonaprenyl-PP were used as polyprenyl donors, but tetraprenyl- and farnesyl-PPs were scarcely transferred to 4-hydroxybenzoic acid. No inhibition was observed by the end-product, ubiquinone-9 of P. putida. Long chain acyl-CoA, free fatty acids, or isopentenyl-PP strongly inhibited the enzyme activity. A possible regulatory role of the enzyme in bacterial ubiquinone biosynthesis is discussed.
- 社団法人日本農芸化学会の論文
- 1991-09-23
著者
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Uchida Koji
Graduate School Of Bioagricultural Sciences Nagoya University
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Uchida K
Soy Sauce Research Laboratory Kikkoman Corp.
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Uchida Kinya
Institute Of Applied Microbiology The University Of Tokyo
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Kawahara Kazyyoshi
Institute Of Applied Microbiology The University Of Tokyo
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KAWAHARA Kazuyoshi
Institute of Applied Microbiology, The University of Tokyo
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KOIZUMI Naohisa
Institute of Applied Microbiology, The University of Tokyo
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KAWAJI Haruhiko
Institute of Applied Microbiology, The University of Tokyo
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OISHI Kunio
Institute of Applied Microbiology, The University of Tokyo
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AIDA Ko
Institute of Applied Microbiology, The University of Tokyo
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Oishi Kunio
Institute Of Applied Microbiology The University Of Tokyo:(present Office)college Of Agriculture And
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Kawaji Haruhiko
Institute Of Applied Microbiology The University Of Tokyo
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Koizumi Naohisa
Institute Of Applied Microbiology The University Of Tokyo
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