Results 11 to 20 of about 50,343 (325)
Plant Physiology, 1997 Abstract We compared the heat-denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase and further examined the ability of Rubisco activase to restore the activity of heat-denatured Rubisco originally reported (E. Sanchez de Jimenez, L. Medrano, and E. Martinez-Barajas [1995] Biochemistry 34:
Nancy A. Eckardt, Archie R. Portis
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Rubisco, Rubisco activase, and global climate change [PDF]
Journal of Experimental Botany, 2008 Global warming and the rise in atmospheric CO(2) will increase the operating temperature of leaves in coming decades, often well above the thermal optimum for photosynthesis. Presently, there is controversy over the limiting processes controlling photosynthesis at elevated temperature.
David S. Kubien +2 more
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Two Residues of Rubisco Activase Involved in Recognition of the Rubisco Substrate [PDF]
Journal of Biological Chemistry, 2005 Rubisco activase is an AAA(+) protein, a superfamily with members that use a "Sensor 2" domain for substrate recognition. To determine whether the analogous domain of activase is involved in recognition of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39), two chimeric activases were constructed, interchanging a Sensor 2-containing
Cishan Li +2 more
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Rubisco in complex with Rubisco large subunit methyltransferase [PDF]
Proceedings of the National Academy of Sciences, 2009 SET domain protein lysine methyltransferases (PKMT) are a structurally unique class of enzymes that catalyze the specific methylation of lysine residues in a number of different substrates. Especially histone-specific SET domain PKMTs have received widespread attention because of their roles in the regulation of epigenetic gene expression and the ...
Roberta Magnani +8 more
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Regulation of Rubisco activase and its interaction with Rubisco [PDF]
Journal of Experimental Botany, 2007 The large, alpha-isoform of Rubisco activase confers redox regulation of the ATP/ADP response of the ATP hydrolysis and Rubisco activation activities of the multimeric activase holoenzyme complex. The alpha-isoform has a C-terminal extension that contains the redox-sensitive cysteine residues and is characterized by a high content of acidic residues ...
Cishan Li +4 more
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Rubisco Assembly in the Chloroplast [PDF]
Frontiers in Molecular Biosciences, 2018 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the rate-limiting step in the Calvin-Benson cycle, which transforms atmospheric carbon into a biologically useful carbon source. The slow catalytic rate of Rubisco and low substrate specificity necessitate the production of high levels of this enzyme.
Anna Vitlin Gruber, Leila Feiz
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Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling
Frontiers in Molecular Biosciences, 2023 Ribulose-1,5-bisphosphate (RuBP) carboxylase-oxygenase (Rubisco) enzyme is the limiting step of photosynthetic carbon fixation, and its activation is regulated by its co-evolved chaperone, Rubisco activase (Rca). Rca removes the intrinsic sugar phosphate inhibitors occupying the Rubisco active site, allowing RuBP to split into two 3-phosphoglycerate ...
Kazi Waheeda +6 more
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Bioscience, Biotechnology, and Biochemistry, 2017 Abstract Since the discovery of its role in the CO2 fixation reaction in photosynthesis, RuBisCO has been one of the most extensively researched enzymes in the fields of biochemistry, molecular biology, and molecular genetics as well as conventional plant physiology, agricultural chemistry, and crop science.
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Does Long-Term Elevation of CO2 Concentration Increase Photosynthesis in Forest Floor Vegetation? (Indiana Strawberry in a Maryland Forest). [PDF]
, 1997 As the partial pressure of CO2 (pCO2) in the atmosphere rises, photorespiratory loss of carbon in C3 photosynthesis will diminish and the net efficiency of light-limited photosynthetic carbon uptake should rise.
Drake, B.G. +3 more
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Effect of light and dark treatments on photosynthetic key enzymes in rice
浙江大学学报. 农业与生命科学版, 2001 After 24 h darkness treatments, Rubisco contents and ratio of Rubisco to soluble protein in the rice seedling increased with illumination rising. When the seedling was put in darkness after 2 h illumination, Rubisco contents decreased at first 20 min ...
JIANG De-an +3 more
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