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. 1985 May;78(1):149–154. doi: 10.1104/pp.78.1.149

Sucrose Synthase of Soybean Nodules

Matthew Morell 1,1, Les Copeland 1
PMCID: PMC1064693  PMID: 16664189

Abstract

Sucrose synthase (UDPglucose: d-fructose 2-α-d-glucosyl transferase, EC 2.4.1.13) has been purified from the plant cytosolic fraction of soybean (Glycine max L. Merr cv Williams) nodules. The native enzyme had a molecular weight of 400,000. The subunit molecular weight was 90,000 and a tetrameric structure is proposed for soybean nodule sucrose synthase. Optimum activity in the sucrose cleavage and synthesis directions was at pH 6 and pH 9.5 respectively, and the enzyme displayed typical Michaelis-Menten kinetics. Soybean nodule sucrose synthase had a high affinity for UDP (Km, 5 micromolar) and a relatively low affinity for ADP (apparent Km, 0.13 millimolar) and CDP (apparent Km, 1.1 millimolar). The Km for sucrose was 31 millimolar. In the synthesis direction, UDPglucose (Km, 0.012 millimolar) was a more effective glucosyl donor than ADPglucose (Km, 1.6 millimolar) and the Km for fructose was 3.7 millimolar. Divalent cations stimulated activity in both the cleavage and synthesis directions and the enzyme was very sensitive to inhibition by heavy metals.

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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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