Sucrose phosphorylase (EC 2.4.1.7)was purified to homogeneity from Leuconostoc mesenteroides cells with a specific activity of 173.8 units per nig protein by ammoniumsulfate fractionation, anion exchange HPLC on TSKgel DEAE-5PW,and hydrophobic HPLCon TSKgel Ether-5PW.The purified enzyme was an acidic protein having an isoelectric point of pH 4.6 and sJo.w °f 4.34 S. The molecular weight of this enzyme was estimated to be 56,400 by sedimentation equilibrium, 55,000 by SDS-polyacrylamide gel electrophoresis, and HPLC gel filtration on TSKgel G3000SW, suggesting that the enzyme is a monomeric protein.With regard to molecular weight, amino acid composition, and N-terminal amino acid sequence of 30 residues, this enzyme is close to the glucosyltransferase A of Streptococcus mutans.
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Koga et al. (1991) studied this question.