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SUCROSE SYNTHASE (UDPGLUCOSE: d-fructose 2-alpha-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 (K(m), 5 micromolar) and a relatively low affinity for ADP (apparent K(m), 0.13 millimolar) and CDP (apparent K(m), 1.1 millimolar). The K(m) for sucrose was 31 millimolar. In the synthesis direction, UDPglucose (K(m), 0.012 millimolar) was a more effective glucosyl donor than ADPglucose (K(m), 1.6 millimolar) and the K(m) 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.
Morell et al. (Wed,) studied this question.