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. 1974 Nov;54(5):752–757. doi: 10.1104/pp.54.5.752

Properties of Glucosyltransferase and Glucan Transferase from Spinach

James C Linden a,1, Widmar Tanner a,2, Otto Kandler a
PMCID: PMC366595  PMID: 16658965

Abstract

A glucosyl and a glucosyl-glucan transferase activity from spinach (Spinacia oleracea L. var. Matador) leaves have been partially purified and characterized. The latter activity (fraction 1 after diethylaminoethylcellulose chromatography) is responsible for the transfer of glucosyl as well as of maltosyl, maltotriosyl, and higher homologous residues to glucose giving rise to maltose and the correspondingly larger molecules. This fraction also shows β-amylase activity. The transfer takes place only to glucose; maltose, as well as other α-1,4-glucans, serve as donors. The enzyme fraction 2 is amylase-free and catalyzes only the transfer of glucosyl moieties, again with high acceptor specificity to glucose. Maltose and larger α-1, 4-glucans, with the exception of maltotriose and maltotetraose, act as donors. The physiological function of these enzymes may be the formation of oligosaccharide primers for starch synthetase or phosphorylase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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