标题：Specificity of a Particulate Glucosyltransferase in Seedlings of Pisum sativum L. Which Catalyzes the Formation of 5'-O-(β-D-Glucopyranosyl)Pyridoxine
期刊名称：Journal of Nutritional Science and Vitaminology
印刷版ISSN：0301-4800
电子版ISSN：1881-7742
出版年度：1982
卷号：28
期号：4
页码：359-366
DOI：10.3177/jnsv.28.359
出版社：Center for Academic Publications Japan
摘要：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.
关键词：pyridoxine 5'-β-glucoside;glucosyltransferase;glucosylation;HPLC of vitamin B6
