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Plant and Cell Physiology, 1979, Vol. 20, No. 4 803-809
© 1979


Article

Alicyclic acid metabolism in plants 12. Partial purification and some properties of shikimate kinase from Phaseolus mungo seedlings

Tomokazu Koshiba

Department of Biology, Tokyo Metropolitan University Setagaya-ku, Tokyo 158, Japan

Shikimate kinase from Phaseolus mungo seedlings was partially purified by DEAEcellulose, hydroxyapatite and Sephacryl S-200 column chromatographies. The activity was completely inhibited by EDTA and the requirement for Mg2+ could be partially replaced by Mn2+, Ca2+; Co2+ and Cd2+. Sulfhydryl inhibitor did not inhibit the enzyme activity. The apparent Km values for shikimic acid and ATP at pH 8.6 were 0.25 mM and 0.38 mM, 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.

(Received January 11, 1979; )
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