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Plant Physiology 66:34-39 (1980)
© 1980 American Society of Plant Biologists

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Articles

Activation of Glyceraldehyde-Phosphate Dehydrogenase (NADP) and Phosphoribulokinase in Phaseolus vulgaris Leaf Extracts Involves the Dissociation of Oligomers

Onnop Wara-Aswapati1, Roger J. Kemble2 and J. William Bradbeer3

Department of Plant Sciences, University of London King's College, 68 Half Moon Lane, London SE24 9JF England

Phosphoribulokinase (EC 2.7.1.19, ATP: D-ribulose-5-phosphate-1-phosphotransferase) resembles the NADPH-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13, D-glyceraldehyde-3-phosphate: NADPH+ oxidoreductase [phosphorylating]) of chloroplasts in that the activation of both of these enzymes involves the dissociation of oligomers (apparently tetrameric forms) with low catalytic activity to give protomers which possess higher catalytic activity. Gel filtration on Sepharose 6B has shown that the molecular weights of the oligomer and active protomer of phosphoribulokinase are, respectively, about 6.8 x 105 and 1.7 x 105, whereas the corresponding values for glyceraldehyde-3-phosphate dehydrogenase are 8.2 x 105 and 2.2 x 105. Activation of both enzymes occurs in response to either ATP, dithiothreitol, or cholate while the glyceraldehyde-3-phosphate dehydrogenase is also activated by NADPH. Activation/dissociation of these enzymes may involve conformational changes resulting from nucleotide binding, the reduction of sulfur bridges, and the cholate induced loosening of hydrophobic interactions.

1 Recipient of a Colombo Plan Studentship. Present address: Department of Biology, Chiengmai University, Chiengmai, Thailand.

2 Recipient of a Science Research Council Studentship. Present address: Plant Breeding Institute, Maris Lane, Trumpington, Cambridge CB2 2LQ U. K.

3 To whom reprint requests should be addressed.




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