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A d-glucosylated form of dextransucrase: Demonstration of partial reactions by Gary A. Luzio; Veena K. Parnaik; Robert M. Mayer is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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A D-glucosylated form of dextransucrase, whose preparation and characteristics have just been reported in Carbohydr. Res., was employed in a series of studies designed to explore the question of whether the bound sugars participate in the reactions catalyzed by the enzyme. When exposed to maltose, a good acceptor-substrate, monomeric D-glucosyl groups were rapidly transferred to the disaccharide, affording a trisaccharide. In the absence of an acceptor, monomeric D-glucose was released from the enzyme by hydrolysis. In a reaction with D-fructose, the charged enzyme catalyzed the formation of sucrose. Finally, in the presence of unlabeled sucrose, monomeric D-glucosyl groups were chased into enzyme-associated oligomers. Evidence is also presented which indicates that the various pathways for the bound D-glucosyl groups are competitive. The significance of these observations is discussed.

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Author

Gary A. Luzio; Veena K. Parnaik; Robert M. Mayer

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0008-6215)

Published

1983

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)