A Novel 3-Dehydroquinate Dehydratase Catalyzing Extracellular Formation of 3-Dehydroshikimate by Oxidative Fermentation of Gluconobacter oxydans IFO 3244
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概要
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In addition to the cytoplasmic soluble form of 3-dehydroquinate dehydratase (sDQD) (EC 4.1.2.10), a novel form of DQD occurring in the periplasmic space was found in Gluconobacter oxydans IFO 3244. The novel DQD, tentatively designated as pDQD, appeared to have a practical function involved in oxidative fermentation extracellularly coupling with membrane-bound quinoprotein quinate dehydrogenase (QDH) yielding 3-dehydroshikimate from quinate via 3-dehydroquinate. pDQD was not detached from the membrane by mechanical disruption or extraction with high salt, but was solubilized only with detergent. pDQD and sDQD were purified to homogeneity and compared as to their enzymatic properties. They showed the same apparent molecular weights and same catalytic properties, but they were distinct each other in subunit molecular mass, 16 kDa for pDQD and 47 kDa for sDQD.
- 社団法人 日本農芸化学会の論文
著者
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TOYAMA Hirohide
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University
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MATSUSHITA Kazunobu
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University
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ADACHI Osao
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University
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ANO Yoshitaka
Department of Biological Chemistry, Faculty of Agricultre, Yamaguchi University
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Takayanagi H
Research Center For Biological Function The Kitasato Institute
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