STUDIES WITH THREE BACTERIAL SUCROSE PHOSPHORYLASES

Abstract

Sucrose phosphorylases of Pseudomonas saccharophila, P. putrefaciens, and Leuconostoc mesenteroides were partially purified and their properties compared. All 3 enzymes are alpha-transgluco-sidases capable of catalyzing the exchange between inorganic phosphate and glucose-1-phosphate. Different concns. of (NH4)2SO4 are required for their precipitation. The enzyme of P. putrefaciens does not react with sorbose or xyloketose as glucosyl acceptors. The phosphorylase of L. mesenteroides is less sensitive to inhibition by glucose than are the other enzymes. In studies with a highly purified enzyme of L. mesenteroides, no requirement for a dissociable cofactor could be found. No stable glucose moiety such as a glucoside, nucleotide derivative, or hexose diphosphate could be detected as part of the postulated enzyme-glucose complex. No reaction between the enzyme and alpha-uridine diphosphoglucose could be shown. Hydrolase activity with both sucrose and glucose-1-phosphate appears to be an intrinsic property of the sucrose phosphorylase of L. mesenteroides.