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Engineering CO<sub>2</sub>-Fixing Carboxysome into <i>Saccharomyces cerevisiae</i> to Improve Ethanol Production. [PDF]
Int J Mol SciLi M +5 more
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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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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).
J Nathan, Henderson +4 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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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 ...
S P, Robinson, A R, Portis
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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 ...
Ragupathi, Nagarajan, Kulvinder S, Gill
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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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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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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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Integrative oncology: Addressing the global challenges of cancer prevention and treatment
Ca-A Cancer Journal for Clinicians, 2022Jun J Mao,, Msce +2 more
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