Results 261 to 270 of about 27,480 (298)
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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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Photosynthesis: Rubisco rescue
Nature Plants, 2015Rubisco catalyses the first step in photosynthetic carbon fixation, but it can be easily poisoned by side-products of its activity. Structural and functional analyses of a protein conserved across plants, algae and bacteria shows how one such blockage is both removed and recycled.
Rebekka M, Wachter, J Nathan, Henderson
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Rubisco: Structure and Mechanism
Annual Review of Biophysics and Biomolecular Structure, 1992CONTENTS PERSPECTIVES AND OVERVIEW 1 1 9 PHYSIOLOGICAL AND GENETIC ASPECTS 120 Photosynthesis and Photorespiration 120 Synthesis and Assembly . . . . . ..... ... . . ... . . . . . . . . . . .. .. 121 CHEMICAL MECHANISM 122 Activation-the Ternary Complex of Enzyme, CO" and Mg( II) 122 Overall Carboxylation Reaction . . . ... . . . . . .
G, Schneider +2 more
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Protein engineering of rubisco
Acta Crystallographica Section B Structural Science, 1991Modification of the kinetic parameters of enzymes by protein engineering requires extensive knowledge of the structural details of the enzyme and its complexes with different reaction intermediate analogues. Such structural studies are described here for Rubisco, ribulose-1,5-bisphosphate carboxylase/oxygenase, which catalyzes the initial reactions of ...
C I, Brändén +2 more
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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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Evolution and origins of rubisco
Current BiologyRubisco (D-ribulose 1,5-bisphosphate carboxylase/oxygenase) is the most abundant enzyme in the world, constituting up to half of the soluble protein content in plant leaves. Such is its ubiquity that its chemical fingerprint can be detected in the geological record spanning billions of years.
Leah J, Taylor-Kearney +2 more
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Complex formation of rubisco and rubisco activase
Biophysical Journal, 2022Kazi Waheeda, Po-Lin Chiu
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1983
Leaf rubisco (Fraction 1 protein) was purified from a number of cruciferous species, and subunit polypeptide patterns were examined by isoelectric focusing in the presence of 8 M urea. Both cultivated and wild Brassica species were studied by this method and results suggest that the protein may be a useful taxonomic marker, especially where species may
M. P. Robbins, J. G. Vaughan
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Leaf rubisco (Fraction 1 protein) was purified from a number of cruciferous species, and subunit polypeptide patterns were examined by isoelectric focusing in the presence of 8 M urea. Both cultivated and wild Brassica species were studied by this method and results suggest that the protein may be a useful taxonomic marker, especially where species may
M. P. Robbins, J. G. Vaughan
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Nature, 2006
Rubisco is said to be both the most important enzyme on Earth and surprisingly inefficient. Yet an understanding of the reaction by which it fixes CO2 suggests that evolution has made the best of a bad job.
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Rubisco is said to be both the most important enzyme on Earth and surprisingly inefficient. Yet an understanding of the reaction by which it fixes CO2 suggests that evolution has made the best of a bad job.
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Rubisco's chiropractor: a study of higher plant Rubisco activase
2015Rubisco activase operates as the chaperone responsible for maintaining the catalytic competency of Ribulose 1,5-bisphophate carboxylase oxygenase (Rubisco) in plants. Rubisco is notoriously inefficient, rapidly self-inactivating under physiological conditions. Rubisco activase uses the power released from the hydrolysis of ATP to power a conformational
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