Specificity of a Particulate Glucosyltransferase in Seedlings of Pisum sativum L. Which Catalyzes the Formation of 5-O-(β-D-Glucopyranosyl)Pyridoxine

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A glucosyltransferase, catalyzing the transfer of D-glucose from UDP-glucose to the 5-hydroxyl group of pyridoxine, was isolated as a particulate enzyme from seedlings of podded pea (Pisum sativum L, cv. Kinusaya). The enzyme required additional Mg2+ for its function. The pH optimum for glucosylation of pyridoxine was between 7.8 and 8.8. The enzyme showed high specificity for UDP-glucose and relative specificity for glucosyl acceptor : pyridoxine was replaceable by pyridoxamine. Several compounds tested other than vitamin B6 failed to serve as the acceptor. It was shown that a methylene group on C-4 participated in the formation of enzyme-substrate complex, and that the rate of glucosylation was dependent upon the C-4 substituent. From the results of kinetic studies and an experiment in vivo, the enzyme was inferred to be UDP-glucose: pyridoxine 5-O-β-glucosyltransferase.
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