Abstract
An enzyme, which catalyzes the isomerization of D-glucose to D-fructose, has been found in a newly isolated bacterium which tentatively identified as Pacacolobacterum aerogenoides. The enzyme converts not only D-glucose but also D-mannose to D-fructose, and NAD and Mg++ are required as cofactor for this isomerization. The properties of this enzyme were sum-marized as follows: (1) As a cofactor for the isomerization by this enzyme, NAD was absolutely necessary, whereas NADP, FMN and FAD were not. (2) The optimum pH was found to be at 7.5 and optinum temperature was at about 40°C. (3) The enzyme activity was markedly reduced by EDTA treatment and the reduced activity by EDTA was restored by the addition of Mg++, Mn++ or Co++. (4) The enzyme activity was strongly inhibited by monoiodoacetate, p-chloromercuribenzoate, and Cu++, however, the activity was recovered by adding cysteine or glutathione.
