Rubisco Activase Mediates ATP-Dependent Activation of Ribulose Bisphosphate Carboxylase
Open Access
- 1 September 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 85 (1) , 152-154
- https://doi.org/10.1104/pp.85.1.152
Abstract
The activation level of ribulosebisphosphate carboxylase following preincubation with ribulose 1,5-bisphosphate was increased by ATP and ribulosebisphosphate carboxylase activase in the absence of thylakoids or illumination. Maximal activation was obtained with 0.5 millimolar ATP in the presence of an ATP regenerating system (phosphoenolpyruvate and pyruvate kinase). Without the ATP regenerating system, activation was lower, linearly dependent on ATP concentration up to 1.0 millimolar, and was strongly inhibited by ADP.This publication has 19 references indexed in Scilit:
- Purification of ribulose-1,5-bisphosphate carboxylase/oxygenase with high specific activity by fast protein liquid chromatographyAnalytical Biochemistry, 1986
- Inhibition of ribulose bisphosphate carboxylase by substrate ribulose 1,5-bisphosphate.Journal of Biological Chemistry, 1983
- Light limitation of photosynthesis and activation of ribulose bisphosphate carboxylase in wheat seedlingsProceedings of the National Academy of Sciences, 1981
- Interaction of sugar phosphates with the catalytic site of ribulose-1,5-bisphosphate carboxylaseBiochemistry, 1981
- A model for the kinetics of activation and catalysis of ribulose 1,5-bisphosphate carboxylaseBiochemical Journal, 1976
- The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implicationsBiochemistry, 1976
- The role of pH in the regulation of carbon fixation in the chloroplast stroma. Studies on CO2 fixation in the light and darkBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
- Regulation of Ribulose 1,5-Diphosphate Carboxylase by Substrates and Other MetabolitesPlant Physiology, 1975
- Activation of Ribulose 1,5-Diphosphate Carboxylase by Nicotinamide Adenine Dinucleotide Phosphate and Other Chloroplast MetabolitesPlant Physiology, 1974
- The inner membrane of the chloroplast envelope as the site of specific metabolite transportBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1971