Phosphorolysis of maltose by enzyme preparations from Neisseria meningitidis.

In previous studies on the utilization of maltose and glucose by lfeisseria meningitidis (meningococcus) it has been found that the disaccharide is utilized more rapidly than glucose (1, 2). Phosphate esterification was observed with growing cultures, washed cells, and cell-free extracts of this organism in the presence of maltose but not of glucose (3). The properties of the phosphate ester appeared to be similar to those of glucose-l-phosphate (4). a-n-Glucose-l-phosphate had been found previously to be the product of the phosphorolysis of sucrose by Pseudomonas saccharophila (5) and Pseudomonas putrejaciens (6). It is also the product of the combined action of the enzymes amylomaltase and phosphorylase of Escherichia coli on maltose (7). It seemed likely, therefore, that a mechanism similar to that of P. saccharophila or E. coli was involved in the decomposition of maltose by the meningococcus. Further investigation of this problem has led to the conclusion that the meningococcal enzyme catalyzes the direct phosphorolysis of maltose but that the phosphoric ester produced is P-n-glucose-l-phosphate (8, 9). The mechanism of action of the enzyme appears to be very different from that of sucrose phosphorylase. The detailed studies on the reversible phosphorolytic cleavage of maltose by the meningococcal enzyme are presented in this paper.