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. 1980 Jul;66(1):34–39. doi: 10.1104/pp.66.1.34

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

Onnop Wara-Aswapati 1,1, Roger J Kemble 1,2, J William Bradbeer 1,3
PMCID: PMC440526  PMID: 16661389

Abstract

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 × 105 and 1.7 × 105, whereas the corresponding values for glyceraldehyde-3-phosphate dehydrogenase are 8.2 × 105 and 2.2 × 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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