Summary: A glycerol-kinase-deficient mutant of was isolated. Genetic analysis revealed that the mutation is located on linkage group VI. The phenotype of this mutant differed from that of a glycerol kinase mutant of in its ability to utilize dihydroxyacetone (DHA). The weak growth on glycerol of the glycerol kinase mutant showed that glycerol phosphorylation is an important step in glycerol catabolism. The mutant could still grow normally on DHA because of the presence of a DHA kinase. This enzyme, probably in combination with an NAD-dependent glycerol dehydrogenase, present only in the mutant, is responsible for the weak growth of the mutant on glycerol. Enzymic analysis of both the mutant and the parental strain showed that at least three different glycerol dehydrogenases were formed under different physiological conditions: the NAD-dependent enzyme described above, a constitutive NADP-dependent enzyme and a -glyceraldehyde-specific enzyme induced on -galacturonate. The glycerol kinase mutant showed impaired growth on -galacturonate.


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