Abstract
A particulate enzyme preparation from Bacillus stearothermophilus synthesized 1, 3-poly (glycerol phosphate) from CDPglycerol at an optimum pH of 8.0 and the reaction was stimulated by divalent cations. Km for CDPglycerol was 0.18mM. The synthesis was inhibited by CMP, CDP, and CTP and by concentrations of CDP-glycerol above 0.49mM. The reaction was irreversible. The product had an average chain length of 8 glycerol units. About two thirds of the polymers were synthesized in entirety while the remainder were attached to some acceptor by their phosphate end. The enzyme was able to synthesize only a limited amount of polymer.
