Purification and Properties of Soluble D-Glucoside 3-Dehydrogenase from Flavobacterium saccharophilum(Biological Chemistry)

概要

論文の詳細を見る
D-Glucoside 3-dehydrogenase [EC 1.1.99.13], which oxidizes validoxylamine A to the 3-keto derivative, was purified from a soluble fraction of Flavobacterium saccharophilum by ion-exchange chromatography and gel filtration. The purified enzyme had a single protein band on disk gel electrophoresis, and FAD, nonheme iron, and acid-labile sulfide were shown to be the prosthetic group. The molecular weight of the enzyme was 65,000 by gel filtration with a Sephacryl S-200 column and 66,000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, indicating that the enzyme is a monomer. The optimum pH for 2,6-dichlorophenolindophenol, phenazine methosulfate, and purified cytochrome c_<551> reductase activity were 6.0,8.0〜9.0, and 7.0, respectively. D-Glucose and methyl α- and β-D-glucoside were converted to the corresponding 3-keto sugars. D-Glucoside 3-dehydrogenase reduced the membrane-bound cytochrome c_<551> with methyl α-D-glucoside, D-glucose, sucrose, or validoxylamine A. This shows that the membrane-bound cytochrome c_<551> may be the in vivo hydrogen acceptor of a soluble D-glucoside 3-dehydrogenase.
社団法人日本農芸化学会の論文
1988-08-23