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Pyruvate Kinase, a Possible Regulatory Enzyme in Higher Plants

Ronald G. Duggleby and David T. Dennis
Plant Physiology
Vol. 52, No. 4 (Oct., 1973), pp. 312-317
Stable URL: http://www.jstor.org/stable/4263367
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Pyruvate Kinase, a Possible Regulatory Enzyme in Higher Plants
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Abstract

A number of plant species were examined for the presence of pyruvate kinase (pyruvate-ATP phosphotransferase, EC 2.7.1.40), and of a phosphatase activity which hydrolyzes phosphoenolpyruvate. Of those examined, only cotton (Gossypium sp. L.) seeds were found to be sufficiently free of the phosphatase to permit a kinetic study of pyruvate kinase. During germination of cotton seeds, pyruvate kinase activity rises for the first 3 days, after which it falls back to its original level. This developmental pattern is characteristic of enzymes involved in the conversion of fat into carbohydrate in fat-storing seeds. The phosphatase also rose rapidly during germination, which precluded the use of extracts from seedlings in the study of pyruvate kinase. No evidence was found for the presence of more than one pyruvate kinase in cotton seedlings. In crude extracts from ungerminated seeds, the enzyme shows slight deviations from normal kinetics with respect to phosphoenolpyruvate, magnesium, and to a lesser extent, ADP. After partial purification of the enzyme by ion exchange chromatography, the enzyme shows normal kinetics. The enzyme is activated by AMP, and inhibited by both ATP and citrate, in both crude and partially purified preparations. It is suggested that cotton seed pyruvate kinase is a regulatory enzyme.

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