The anomeric specificity of β-galactosidase and lac permease from Escherichia coli

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Abstract
.beta.-Galactosidase acted on .alpha.-lactose slightly more than twice as rapidly as on .beta.-lactose for both the hydrolysis and transgalactosylis reactions. The effect was on the Vmax values; the Km values for the different anomeric forms were the same. The step of the raction for which the enzyme has anomeric specificity was glycosidic bond breakage. The steps in glucose release or in the glucose acceptor reaction were not affected by anomeric composition. Neither allolactose hydrolysis nor transport of lactose into the cells by lac permease was sensitive to the anomeric composition of the substrate. The implications of these results for lac operon induction and for lactose metabolism are discussed.