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Plant Physiology 60:548-553 (1977)
© 1977 American Society of Plant Biologists

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Occurrence and Properties of Polygalacturonase in Avena and Other Plants

Russell Pressey and Jimmy K. Avants

Agricultural Research Service, United States Department of Agriculture, Richard B. Russell Research Center Athens, Georgia 30604

Polygalacturonase activity has been detected in a number of plants including seedlings of Phaseolus vulgaris, Zea mays, Avena sativa, and Pisum sativum. Particular emphasis was placed on characterizing the enzyme from oat seedlings. This enzyme is solubilized by 0.2 M NaCl, and its activity is highest near the apical tips of oat coleoptiles. It has a pH optimum between 5 and 5.5 and is activated by Ca2+, with an optimal concentration of 0.4 mM. Cd2+ also activates the enzyme but less effectively than Ca2+. The rate of attack is maximal for substrates with chain lengths of about 20 units and slowest for digalacturonate. The oat enzyme hydrolyzes galacturonans by removing galacturonic acid units from the nonreducing ends and progressively shortens the substrate chains.




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T. Yang, L. Bar-Peled, L. Gebhart, S. G. Lee, and M. Bar-Peled
Identification of Galacturonic Acid-1-phosphate Kinase, a New Member of the GHMP Kinase Superfamily in Plants, and Comparison with Galactose-1-phosphate Kinase
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K. A. Hadfield and A. B. Bennett
Polygalacturonases: Many Genes in Search of a Function
Plant Physiology, June 1, 1998; 117(2): 337 - 343.
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Copyright © 1977 by the American Society of Plant Biologists