Results 161 to 170 of about 2,338 (183)
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Structure ofArabidopsis thalianaRubisco activase
Acta Crystallographica Section D Biological Crystallography, 2015The CO2-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is inactivated by the formation of dead-end complexes with inhibitory sugar phosphates. In plants and green algae, the ATP-dependent motor protein Rubisco activase restores catalytic competence by facilitating conformational changes in Rubisco that promote the release of ...
Dirk Hasse +2 more
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Evolution of Rubisco activase gene in plants
Plant Molecular Biology, 2017Rubisco activase of plants evolved in a stepwise manner without losing its function to adapt to the major evolutionary events including endosymbiosis and land colonization. Rubisco activase is an essential enzyme for photosynthesis, which removes inhibitory sugar phosphates from the active sites of Rubisco, a process necessary for Rubisco activation ...
Kulvinder S. Gill, Ragupathi Nagarajan
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The activity of Rubisco’s molecular chaperone, Rubisco activase, in leaf extracts
Photosynthesis Research, 2011Rubisco frequently undergoes unproductive interactions with its sugar-phosphate substrate that stabilize active sites in an inactive conformation. Restoring catalytic competence to these sites requires the "molecular chiropractic" activity of Rubisco activase (activase).
Carmo-Silva, A. Elizabete +1 more
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Rubisco Activase Activity Assays
2010Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) activase functions as a mechano-chemical motor protein using the energy from ATP hydrolysis to contort the structure of its target protein, Rubisco. This action modulates the activation state of Rubisco by removing tightly-bound inhibitory sugar-phosphates from Rubisco's catalytic sites ...
Barta, Csengele +2 more
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Biophysical characterization of higher plant Rubisco activase
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013Rubisco activase (Rca) is a chaperone-like protein of the AAA+ family, which uses mechano-chemical energy derived from ATP hydrolysis to release tightly bound inhibitors from the active site of the primary carbon fixing enzyme ribulose 1,5-bisphosphate oxygenase/carboxylase (Rubisco).
Suratna Hazra +4 more
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The regulation of Rubisco by Rubisco activase
Journal of Experimental Botany, 1995Abstract The activity of Rubisco depends on the conversion of the inactive form (E) to the active form (ECM); the binding of the inhibitors CA1P and RuBP to ECM and E, respectively; and the catalytic formation of inhibitory sugar bisphosphates from the enediol intermediate that precedes carboxylation/oxygenation.
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Rubisco activase - Rubisco's catalytic chaperone.
Photosynthesis research, 2003The current status of research on the structure, regulation, mechanism and importance of Rubisco activase is reviewed. The activase is now recognized to be a member of the AAA(+) family, whose members participate in macromolecular complexes that perform diverse chaperone-like functions.
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Adenosine triphosphate hydrolysis by purified rubisco activase
Archives of Biochemistry and Biophysics, 1989Activation of ribulose bisphosphate carboxylase/oxygenase (rubisco) in vivo is mediated by a specific protein, rubisco activase. In vitro, activation of rubisco by rubisco activase is dependent on ATP and is inhibited by ADP. Purified rubisco activase hydrolyzed ATP with a specific activity of 1.5 mumol min-1 mg-1 protein, releasing approximately ...
Simon P. Robinson, Archie R. Portis
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Planta, 1996
Transgenic tobacco (Nicotiana tabacum L. cv. W38) plants with an antisense gene directed against the mRNA of ribulose-1,5-bisphosphate carboxylase/ oxygenase (Rubisco) activase were used to examine the relationship between CO2-assimilation rate, Rubisco carbamylation and activase content.
Susanne von Caemmerer +4 more
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Transgenic tobacco (Nicotiana tabacum L. cv. W38) plants with an antisense gene directed against the mRNA of ribulose-1,5-bisphosphate carboxylase/ oxygenase (Rubisco) activase were used to examine the relationship between CO2-assimilation rate, Rubisco carbamylation and activase content.
Susanne von Caemmerer +4 more
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Heat sensitivity of Rubisco, Rubisco activase and Rubisco binding protein in higher plants
Acta Physiologiae Plantarum, 2004During the past few years the investigations concerning Rubisco and the changes of its activity and properties at elevated temperature were reconsidered with special reference to the important role of Rubisco activase and Rubisco binding protein. The major changes in Rubisco, Rubisco activase and Rubisco binding protein reported recently are presented ...
Klimentina Demirevska-Kepova, Urs Feller
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