Results 21 to 30 of about 53,466 (334)
The Catalytic Role of RuBisCO for in situ CO2 Recycling in Escherichia coli
Frontiers in Bioengineering and Biotechnology, 2020 Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is a key enzyme responsible for biological CO2 assimilation. RuBisCO can be heterologously expressed in Escherichia coli so that glucose and CO2 are co-metabolized to achieve high mixotrophic ...
Ju-Jiun Pang +3 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 ...
Raunser, Stefan +6 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 ...
Archie R, Portis +3 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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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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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 CO 2 -fixing enzyme Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) to release tightly bound sugar phosphates. Higher plant Rca is a crop improvement target, but
Devendra Shivhare +3 more
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Pesquisa Agropecuária Brasileira, 2009 The objective of this work was to evaluate photoprotective mechanisms related to low positive temperatures in Coffea canephora (Conilon clones 02 and 153) and C. arabica ('Catucaí' IPR 102) genotypes, involved in cold temperature tolerance. To accomplish
Fábio Luiz Partelli +6 more
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Rubisco : easy purification and immunochemical determination [PDF]
, 2001 Rubisco (Ribulose-1.5-bisphosphate carboxylase/oxygenase) from spinach was purified to homogeneity in one step by gel filtration. This enzyme is suitable for the generation of a specific antibody in rabbits.
Groß, Ulrich
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Plants, 2019 Recent in vivo assays of the responses of Rubisco to temperature in C3 plants have revealed substantial diversity. Three cultivars of soybean (Glycine max L.
James Bunce
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Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro
Molecules, 2022 This study investigated the principal leaf protein (rubisco) solubilization and in vitro ruminal enzyme activity in relation to the molecular structure of proanthocyanidins extracted from leaves of Anogeissus pendula and Eugenia jambolana.
Sultan Singh +6 more
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