Alicyclic acid metabolism in plants 12. Partial purification and some properties of shikimate kinase from Phaseolus mungo seedlings
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Shikimate kinase from Phaseolus mungo seedlings was partially purified by DEAE-cellulose, hydroxyapatite and Sephacryl S-200 column chromatographies. The activity was completely inhibited by EDTA and the requirement for Mg^<2+> could be partially replaced by Mn^<2+>, Ca^<2+>, Co^<2+> and Cd^<2+>. Sulfhydryl inhibitor did not inhibit the enzyme activity. The apparent Km values for shikimic acid and ATP at pH 8.6 were 0.25 m_M and 0.38 m_M, respectively. The activity appeared to be maximal at pH 8.6-9.0. Shikimate-3-phosphate and ADP inhibited the activity slightly. Aromatic amino acids, quinic acid and dehydroquinic acid had no significant effect on the activity.
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