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Plant Physiology 82:1040-1044 (1986)
© 1986 American Society of Plant Biologists

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3-Deoxy-D-arabino-Heptulosonate 7-Phosphate Synthase from Potato Tuber (Solanum tuberosum L.) 1

Jose E. B. P. Pinto2, Joann A. Suzich3 and Klaus M. Herrmann

Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907

3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase, the first enzyme of the shikimate pathway, was purified to electrophoretic homogeneity from tubers of Solanum tuberosum L. cv Superior. The enzyme is a dimer with a native molecular weight of 110,000. The enzyme appears to be hysteretic. The enzyme activity is stimulated by Mn2+ and L-tryptophan. Chromatofocusing resolved two forms of the enzyme with isoelectric points of 7.8 and 8.4, respectively. The enzyme closely resembles an analogous activity previously isolated from roots of Daucus carota (JA Suzich, JFD Dean, KM Herrmann 1985 Plant Physiol 79: 765-770).

2 Present address: Escola Superior de Agricultura de Lavras, Minas Gerais, Brazil.

3 Present address: Department of Botany, University of Minnesota, St. Paul, MN.

1 Supported by a Brazilian Coordenacao do Aperfeicoamento de Pessoal de Nivel Superior to J. E. B. P. P., a Purdue Agricultural Experiment Station Fellowship to J. A. S., and United States Department of Agriculture Grant GAM-8400607 to K. M. H. This is Journal Paper No. 10,579 from the Purdue University Agricultural Experiment Station.




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R. Entus, M. Poling, and K. M. Herrmann
Redox Regulation of Arabidopsis 3-Deoxy-D-arabino-Heptulosonate 7-Phosphate Synthase
Plant Physiology, August 1, 2002; 129(4): 1866 - 1871.
[Abstract] [Full Text] [PDF]


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Copyright © 1986 by the American Society of Plant Biologists