Abstract
Dihydropteroate synthetase purified from pea seedlings catalyzed the formation of dihydropteroic acid from 2-amino-4-hydroxy-6-hydroxymethyldi-hydropteridine and p-aminobenzoic acid in the presence of ATP and Mg2+. The reaction was stimulated by preincubation of the enzyme with hydroxymethyldihydropteridine, ATP and Mg2+. AT32P was incorporated into the enzyme frac tion by incubation with ATP-γ-32P, hydroxymethyldihydropteridine and Mg2+. Dihydropteroic acid was formed and pyrophosphate was liberated by the incubation with p-aminobenzoic acid from the AT32P-incorporated enzyme solution. AMP was detected as the other product in the reaction.The proposed systematic name of dihydropteroate synthetase is discussed.
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