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Description:
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The enzymatic carboxylation of phosphoenolpyruvate by cell free extracts of Neisseria gonorrhoeae was examined and determined to be similar to the reaction catalysed by phosphoenolpyruvate carboxylase (PEPC ) . This is shown by the irreversibility of the reaction and nucleotide independency . The enzyme extract was found to have some characteristics different from the other bacterial PEPC's reported . The enzyme extract showed catalytic activity in the presence of cobalt ions as well as magnesium and manganese ions , was not inhibited by succinate in fresh extracts , and displayed a low Michaelis constant for bicarbonate (0 .59 mM ) as compared to other PEPC's . The significance of this low Michaelis constant is discussed with respect to the growth of the organism and the importance of this enzyme to protein and nucleic acid synthesis . |