Results 11 to 20 of about 27,480 (298)
Photosynthesis Research, 2013 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is prone to inactivation from non-productive binding of sugar-phosphates. Reactivation of Rubisco requires conformational remodeling by a specific chaperone, Rubisco activase.
Spreitzer, R. J. +12 more
core +3 more sources
Rubisco, Rubisco activase, and global climate change [PDF]
Journal of Experimental Botany, 2008 Global warming and the rise in atmospheric CO2 will increase the operating temperature of leaves in coming decades, often well above the thermal optimum for photosynthesis.
Way, Danielle A. +2 more
core +4 more sources
Bioscience, Biotechnology, and Biochemistry, 2017 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 ...
Akiho Yokota
core +3 more sources
Heat sensitivity of Rubisco, Rubisco activase and Rubisco binding protein in higher plants
Acta Physiologiae Plantarum, 2004 During 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.
Demirevska-Kepova, K, Feller, Urs
core +2 more sources
Immunogold localization of Rubisco and Rubisco activase in leaves of rice
浙江大学学报. 农业与生命科学版, 2003 The enzymes of Rubisco and Rubisco activase were localized using immunogold-labeled method and electron microscope techniques. The results showed that Rubisco was mainly located in choloroplast, Rubisco activase, however, specially labeled both in ...
WANG Ni-yan +4 more
doaj +2 more sources
Probing the rice Rubisco-Rubisco activase interaction via subunit heterooligomerization [PDF]
Proceedings of the National Academy of Sciences, 2019 During photosynthesis the AAA+ protein and essential molecular chaperone Rubisco activase (Rca) constantly remodels inhibited active sites of the CO₂-fixing enzyme Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) to release tightly bound sugar ...
Ng, Jediael +3 more
core +4 more sources
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 ...
Raunser, Stefan +6 more
openaire +4 more sources
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 ...
Archie R, Portis +3 more
openaire +2 more sources
Rubisco activation by wheat Rubisco activase isoform 2β is insensitive to inhibition by ADP [PDF]
, 2019 Rubisco activase (Rca) is a catalytic chaperone that remodels the active site, promotes the release of inhibitors and restores catalytic competence to Rubisco.
Degen, G. +3 more
core +1 more source