Glycerol Dehydrogenase and Glycerol Dissimilation in Cellulomonas sp. NT3060

Abstract

Glycerol kinase and glycerol 3-phosphate (G3P) dehydrogenase activities were induced when Cellulomonas sp. NT3060, a high level producer of glycerol dehydrogenase, was grown on either glycerol or G3P. Eleven glycerol-negative mutants were isolated from the wild type strain. These mutant strains were classified into three groups which are defective in glycerol kinase, G3P dehydrogenase and both the enzymes, respectively. All the mutant strains were unable to grow on glycerol, but still showed high glycerol dehydrogenase activity. Gluconate enhanced the formation of glycerol dehydrogenase. A glycerol dehydrogenase-defective mutant strain derived from a mutant strain defective in both glycerol kinase and G3P dehydrogenase showed apparently the sajne growth as the wild type and its parental strains when grown on gluconate. The results indicate that glycerol dehydrogenase does not participate in the dissimilation of glycerol via the phos-phorylative pathway in which glycerol is phosphorylated by glycerol kinase to G3P followed by oxidation to dihydroxyacetone phosphate by G3P dehydrogenase in Cellulomonas sp. NT3060. The physiological role of glycerol dehydrogenase in the strain was discussed.