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Mutants ofStaphylococcus aureus were isolated which were unable to utilized -galactose or lactose, but which were able to utilize all other carbohydrates tested. Growth of the mutants on a peptone-containing medium was inhibited byd -galactose. Of those mutants selected for further study, one (tagI2 ) was missingd -galactose 6-phosphate isomerase, one (tagK3 ) was missingd -tagatose 6-phosphate kinase, and one (tagA4 ) was missingd -tagatose 1, 6-diphosphate aldolase. Each of these mutants accumulated the substrate of the missing enzyme intracellularly. Spontaneous revertants of each of the mutants simultaneously regained their ability to utilized -galactose and lactose, lost their sensitivity tod -galactose, regained the missing enzymatic activities, and no longer accumulated intermediates of thed -tagatose 6-phosphate pathway. These data support our previous contention that the physiologically significant route for the metabolism ofd -galactose and thed -galactosyl moiety of lactose inS. aureus is thed -tagatose 6-phosphate pathway. Furthermore, a mutant constitutive for all three enzymes of this pathway was isolated, indicating that the products of thetagI, tagK , andtagA genes are under common genetic control. This conclusion was supported by the demonstration thatd -galactose 6-phosphate isomerase,d -tagatose 6-phosphate kinase, andd -tagatose 1, 6-diphosphate aldolase are coordinately induced in the parental strain.

journal of bacteriology

Genetic Evidence for the Physiological Significance of the <scp>d</scp> -Tagatose 6-Phosphate Pathway of Lactose and <scp>d</scp> -Galactose Degradation in <i>Staphylococcus aureus</i>

Genetic Evidence for the Physiological Significance of the d -Tagatose 6-Phosphate Pathway of Lactose and d -Galactose Degradation in Staphylococcus aureus