Kinases in Leuconostoc mesenteroides

Abstract

Enzyme extracts of Leuconostoc mesenteroides were found to contain at least four separate kinases: one active with glucose, glucosamine, and N-acetylglucosamine; one active with fructose and mannose; and two active with gluconate, one constitutive and one inducible. The molecular sizes of all the kinases, estimated from sucrose gradient centrifugation, are about the same, 37,000 to 50,000 daltons, except the constitutive gluconate kinase, which is about 100,000 daltons. Apparent Michaelis constants were calculated for all of the substrates mentioned. The kinases are separable on triethylaminoethyl cellulose.

The purification and characterization of glucokinase from the thermophile Bacillus stearothermophilus

“…Glucokinase from B. stearothermophilus demonstrated a requirement for a bivalent cation, as observed for the enzyme from other sources (Fromm & Zewe, 1962;Saito, 1965;DeMoss, 1968;Porter et al, 1980). However, the enzyme from S. mutans OMZ70 differed in its cation requirement, in that Mn2+ and Co2+ were more effective than Mg2+, giving 173 and 264% activity respectively, and Zn2+ and Ca2+ also induced glucokinase activity, of 56 and 34%O respectively.…”

N-Acetylation of Glucosamine-6-Phosphate in Leuconostoc mesenteroides

“…Identification of product. The product obtained from the reaction mixture containing potassium acetate, glucosamine-6-phosphate, and acetylase was compared with that obtained from a reaction mixture containing N-acetylglucosamine, ATP, and the appropriate phosphotransferase (5). The reaction mixtures were subjected to purification procedures and tests in parallel.…”