Purification and properties of NADP-dependent shikimate dehydrogenase from Gluconobacter oxydans IFO 3244 and its application to enzymatic shikimate production.
NADP-Dependent shikimate dehydrogenae (SKDH, EC 1.1.1.25) was purified from Gluconobacter oxydans IFO 3244. SKDH showed a single protein band on native-PAGE accompanying enzyme activity. It required NADP exclusively and catalyzed only the shuttle reaction between shikimate and 3-dehydroshikimate. The optimum pH for shikimate oxidation and 3-dehydroshikimate reduction was found at pH 10 and 7 respectively. SKDH proved to be a useful catalyst for shikimate production from 3-dehydroshikimate.
Adachi
Osao
O
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi, Japan. osao@yamaguchi-u.ac.jp
Ano
Yoshitaka
Y
Toyama
Hirohide
H
Matsushita
Kazunobu
K
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism*; D020600:Gluconobacter oxydans / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D009249:NADP / Q000378:metabolism*; D010084:Oxidation-Reduction; D012765:Shikimic Acid / Q000031:analogs & derivatives / Q000378:metabolism*
D012765:Shikimic Acid; D009249:NADP; D000429:Alcohol Oxidoreductases; C022641:Shikimate dehydrogenase