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ß-1,3-Oligoglucan:Orthophosphate Glucosyltransferase from Euglena gracilis

From the ¹ From the Instituto de Investigaciones Bioquímicas, "Fundación Campomar" and Facultad de Ciencias Exactas y Naturales, Obligado 2490, Buenos Aires 28, Argentina

An enzyme isolated from Euglena gracilis was shown to catalyze the following reversible reaction.

Laminaribiose + inorganic phosphate glucose + glucose 1-phosphate

It also phosphorolyzes the tri-, tetra-, and pentasaccharide. In the direction from right to left, several phosphoric esters could not substitute for -d-glucose 1-phosphate. Glucose, on the contrary, may be replaced by a number of ß-glucosyl derivatives. In the case of arbutin, it was confirmed that the enzyme adds a ß-glucosyl residue in position 3 of the sugar moiety.

No exchange between glucose 1-phosphate and ³²P, or between laminaribiose and ¹⁴C-glucose, in the absence of the other reactants, could be detected. The arsenolysis of laminaribiose was observed, but not that of glucose 1-phosphate.

The purification and some kinetic properties of the enzyme are described. The equilibrium constants for the phosphorolysis of laminaribiose, laminaritriose, and laminaritetraose have been determined and shown to be very similar.

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