Glycolaldehyde Dehydrogenase, an Enzyme Related to Vitamin B₆ Biosynthesis, from Bacillus subtilis

Abstract

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.