SUMMARY: Choline, a component of the wall teichoic acid of , was converted to cytidine diphosphocholine via choline phosphate by enzymes which were identified in cell-free extracts of the pneumococcus. The first enzyme, choline kinase, was investigated in some detail. It appeared to have a pH optimum of 7.3 to 7.4 and was stimulated by Mg. Kinetic studies gave an apparent Michaelis constant ( ) for ATP of 1 mM, and for choline of 0.19 mM, with values of 3 nmol min (mg protein) and 0.5 nmol min (mg protein) respectively. The second enzyme, CDPcholine pyrophosphorylase was specific for CTP and had a requirement for Mg with an optimum at 7 mM.


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