A novel 3-dehydroquinate dehydratase catalyzing extracellular formation of 3-dehydroshikimate by oxidative fermentation of Gluconobacter oxydans IFO 3244.
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.
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Japan. osao@yamaguchi-u.ac.jp
Osao
O
Adachi
Yoshitaka
Y
Ano
Hirohide
H
Toyama
Kazunobu
K
Matsushita
D019342:Acetic Acid / Q000378:metabolism; D002384:Catalysis; D002462:Cell Membrane / Q000201:enzymology; D005285:Fermentation; D020576:Gluconobacter / Q000201:enzymology*; D006836:Hydro-Lyases / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D010084:Oxidation-Reduction; D012765:Shikimic Acid / Q000031:analogs & derivatives* / Q000378:metabolism; D012995:Solubility; D013347:Subcellular Fractions / Q000201:enzymology
C096387:3-dehydroshikimate; D012765:Shikimic Acid; D006836:Hydro-Lyases; C020000:3-dehydroquinate dehydratase; D019342:Acetic Acid