抄録
Glycolaldehyde dehydrogenase was partially purified from Bacillus subtilis IFO 3007. The enzyme was separated into two fractions by DEAE-cellulose column chromatography. These fractions behaved differently in substrate specificities and other properties.
Both the change of vitamin B6 content (ΔB6/Δt) and the activity of glycolaldehyde dehydrogenase reached simultaneously to the maximum values at the early stationary phase. Although none of compounds of vitamin B6 family affected the enzyme activity, the formation of the enzyme was repressed by the addition of pyridoxal 5'-phosphate. The repression increased with the increased concentration of pyridoxal 5'-phosphate and reached about 30 at the concentration of 20 μM. These results that glycolaldehyde dehydrogenase of B. subtilis is closely related to vitamin B6 biosynthesis.
