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. 1972 Sep;50(3):371–374. doi: 10.1104/pp.50.3.371

The Formation of β, 1 → 4 Glucan from UDP-α-d-Glucose Catalyzed by a Phaseolus aureus Enzyme 1

A F Clark a, C L Villemez a
PMCID: PMC366144  PMID: 16658176

Abstract

Particulate enzyme preparations from Phaseolus aureus hypocotyls catalyze the formation of an alkali insoluble β, 1 → 4 linked [14C]-glucan using UDP-α-d [14C]-glucose as substrate. Particulate enzymes prepared from root tissue also catalyzed the production of β, 1 → 4 glucan. UDP-β-d-[14C]-glucose would not serve as a substrate for these enzymes. The presence or absence of β, 1 → 4 glucan synthetase activity was independent of tissue source, substrate concentration, or homogenization method.

The particulate enzyme also catalyzes the formation of a β, 1 → 3 linked glucan from UDP-d glucose which is usually soluble in hot alkali. The solubility of the β, 1 → 3[14C]-glucan decreased when the enzyme was obtained from hypocotyls germinated at a higher temperature. The water-soluble material resulting from the catalyzed reaction includes a large proportion of what appears to be [14C]-laminaribiose, and smaller proportions of [14C]-laminaritriose and [14C]-glucose. There is no detectable quantity of [14C]-cellobiose or [14C]-cellotriose in the water-soluble material.

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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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