Activation of interspecies-hybrid Rubisco enzymes to assess different models for the Rubisco–Rubisco activase interaction [PDF]
, 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
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Heat sensitivity of Rubisco, Rubisco activase and Rubisco binding protein in higher plants [PDF]
, 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
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
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The relative abundance of wheat Rubisco activase isoforms is post‑transcriptionally regulated [PDF]
, 2021 Diurnal rhythms and light availability affect transcription–translation feedback loops that regulate the synthesis of photosynthetic proteins. The CO2-fixing enzyme Rubisco is the most abundant protein in the leaves of major crop species and its activity
Buchner, P. H. +2 more
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Rubisco folding and oligomeric assembly: Detailed analysis of an assembly intermediate [PDF]
, 2011 To become biologically active, a protein must fold into a distinct three-dimensional structure. Many non-native proteins require molecular chaperones to support folding and assembly.
Windhof, A., Windhof, Amanda
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Moderately High Temperatures Inhibit Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (Rubisco) Activase-Mediated Activation of Rubisco [PDF]
, 1998 We tested the hypothesis that light activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is inhibited by moderately elevated temperature through an effect on Rubisco activase.
Crafts-Brandner, Steven J. +2 more
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Specific RubisCO activities of yet uncultured Proteobacteria depending on flanking genes
, 2021 Here we used the first solely activity-based approach for identifying RubisCO active fosmid clones from a metagenomic library. Hydrothermal vent fluids derived from the interface zone between hot fluids emanating from Drachenschlund and ambient cold ...
Perner, Mirjam, Böhnke-Brandt, Stefanie
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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 +1 more source
Журнал органічної та фармацевтичної хімії, 2021 Aim. To isolate and purify protein complexes – ATP synthase and RuBisCO – from pea leaf chloroplasts and study the effect of a microbiological fertilizer “Extracon” and sulfonamide inhibitors acetazolamide and ethoxyzolamide on the enzymatic activity of ...
Andriy V. Semenikhin +3 more
doaj +1 more source
Biochemical characterization of predicted Precambrian RuBisCO [PDF]
, 2016 The antiquity and global abundance of the enzyme, RuBisCO, attests to the crucial and longstanding role it has played in the biogeochemical cycles of Earth over billions of years.
Andralojc, P. John +11 more
core +1 more source