Purification and properties of D-arabinokinase from Propionibacterium pentosaceum.

Reports on the bacterial utilization of u-arabinose have shown two pathways of dissimilation. The first, reported by Cohen (l), demonstrated that Escherichia coli first isomerized n-arabinose to n-ribulose, which was then phosphorylated. A later report by Doudoroff et al. (2) showed that Pseudomonas saccharophi&a oxidized n-arabinose to n-arabonolactone, which was subsequently hydrolyzed to the free arabonic acid and then cleaved into a 2 and a 3 carbon compound. The present report describes a third mechanism of utilization, i.e. the direct phosphorylation of n-arabinose. In addition, the purification and some of the properties of a n-arabinokinase present in Propionibacterium pentosaceum strain El4 are described.