Abstract
The biosynthesis of cholesteryl glucoside by Mycoplasma gallinarum strain J proceeds by the transfer of glucose from uridine-5′-diphosphoglucose to membrane-bound sterol. Galactose also can be coupled to cholesterol via uridine-5′-diphosphogalactose. The reaction is specific for the uridine-5′-diphospho sugars. Enzymatic activity is associated with the membrane. Treatment of the membrane to remove endogenous sterol inactivates the enzyme. Only sterol which has been bound to the membrane participates in the reaction. The optimum pH is about 8.0, and Mg2+ is required. The reaction is unaffected by nucleotide triphosphate, uridine-5′-monophosphate, and uridine-5′-diphosphate. Reduction of pH to the optimum for β-glucosidase in the membrane results in loss of synthesized glucoside. The enzyme is saturated at 0.5 mm uridine-5′-diphosphoglucose. The apparent Km of 2.05 × 10−7 indicates a high affinity of the enzyme for the nucleotide sugar.
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