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. 1976 Nov;58(5):675–680. doi: 10.1104/pp.58.5.675

Membrane-bound UDP-Glucose

Lipid Glucosyltransferases from Peas 1

Rafael Pont Lezica a,2, Pedro A Romero b,3, Marcelo A Dankert b
PMCID: PMC542281  PMID: 16659742

Abstract

An enzymic preparation from peas (Pisum satisum), able to form neutral and polar glycosides, is described. The best sugar donor is UDP-glucose and the acceptors are present in the enzymic system.

The neutral glycolipids have been characterized as steryl and acylated steryl glucosides. The polar glucolipid had been identified as polyprenyl monophosphate glucose. The glucose is linked to the phosphate in β configuration. Polar glucolipids are also formed from UDP-glucose and exogenous prenylic acceptors, either α-saturated, as dolichyl monophosphate, or allylic, as ficaprenyl monophosphate.

The two glucosylating activities have been partially separated by differential centrifugation: the fraction that precipitates at 25,000g has most of the neutral glucolipid-synthesizing activity, and the fraction that sediments at 100,000g is rich in polar glucolipid glucosyl transferase activity. This latter activity was strongly dependent on Mg2+ concentration, the optimum being around 5 to 10 mm. UDP inhibits the reaction and 0.2 to 0.5% (v/v) Triton X-100 has a stimulatory effect. The optimum pH is 7.5.

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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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