Sucrose synthase (EC 2.4.1.13) was purified from peach fruit (Prunus persica) to a single band of protein on SDS-PAGE by ammonium sulfate fractionation, DEAE-cellulose (DE-52) chromatography, Sepharose CL-6B gel filtration, PBA-60 affinity chromatography and Sephadex G-200 gel filtration. The molecular weight was estimated to be 360,000 by gel filtration. The enzyme was found to be a tetramer of identical 87-kDa subunits. The maximum activity for the synthesis and cleavage of sucrose was observed at pH 8.5 and pH 7.0, respectively. The enzymatic reaction followed typical Michaelis-Menten kinetics in both directions, with the following parameters: Km(fructose), 4.8 mmM; Km(UDPglucose), 0.033 mM; Km(sucrose), 62.5 mM; Km(UDP), 0.080 mM. Other properties, such as substrate specificity and the effects of divalent cations, were also investigated. The relationship between the enzyme and the accumulation of sucrose in peach fruit is discussed.
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Moriguchi et al. (1988) studied this question.