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phytochemistry (151) 151
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ribulosebisphosphate carboxylase (143) 143
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1. Full Text Crystal Structure of Carboxylase Reaction-oriented Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase from a Thermophilic Red Alga, Galdieria partita
by Hajime Sugawara and Hiroki Yamamoto and Naoki Shibata and Tsuyoshi Inoue and Sachiko Okada and Chikahiro Miyake and Akiho Yokota and Yasushi Kai
Journal of Biological Chemistry, ISSN 0021-9258, 05/1999, Volume 274, Issue 22, pp. 15655 - 15661
Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39 ) obtained from a thermophilic red alga Galdieria partita has the highest specificity... 
BISPHOSPHATE | SUBSTRATE-SPECIFICITY FACTOR | PYLAIELLA-LITTORALIS | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RIBULOSEBISPHOSPHATE CARBOXYLASE | SPINACH RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | SMALL SUBUNITS | SITE-DIRECTED MUTAGENESIS | CARBON-DIOXIDE | PYROCOCCUS-FURIOSUS | Pentosephosphates - chemistry | Amino Acid Sequence | Ribulose-Bisphosphate Carboxylase - chemistry | Algal Proteins - chemistry | Ribulosephosphates - chemistry | Molecular Sequence Data | Crystallography, X-Ray | Sequence Alignment | Hydrogen Bonding | Sugar Alcohols - chemistry | Protein Conformation | Molecular Structure | Eukaryota - enzymology | Binding Sites
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2. Full Text Ribulose-1,5-Bis-Phosphate Carboxylase/Oxygenase Accumulation Factor1 Is Required for Holoenzyme Assembly in Maize
by Leila Feiz and Rosalind Williams-Carrier and Katia Wostrikoff and Susan Belcher and Alice Barkan and David B. Stern
The Plant Cell, ISSN 1040-4651, 8/2012, Volume 24, Issue 8, pp. 3435 - 3446
Most life is ultimately sustained by photosynthesis and its rate-limiting carbon fixing enzyme, ribulose-1,5-bis-phosphate carboxylase/oxygenase (Rubisco).... 
Proteins | Enzymes | Messenger RNA | Chloroplasts | Gels | RESEARCH ARTICLES | Corn | Plants | Chaperonins | Plant cells | Seedlings | ARABIDOPSIS-THALIANA | HEXADECAMERIC RUBISCO | BUNDLE-SHEATH DEFECTIVE2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MESOPHYLL CHLOROPLASTS | RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE | PLANT SCIENCES | CELL BIOLOGY | LARGE-SUBUNIT | MESSENGER-RNA | CHLOROPLAST BIOGENESIS | RIBULOSE-BISPHOSPHATE CARBOXYLASE | Chloroplasts - enzymology | Chloroplast Proteins - genetics | Molecular Chaperones - metabolism | Genes, Plant | Ribulose-Bisphosphate Carboxylase - genetics | Zea mays - enzymology | Molecular Sequence Data | Genetic Complementation Test | Holoenzymes - metabolism | Escherichia coli - metabolism | Gene Expression Regulation, Plant | Plant Proteins - metabolism | Chloroplasts - genetics | Recombinant Proteins - metabolism | Amino Acid Sequence | Zea mays - genetics | Electrophoresis, Polyacrylamide Gel | Molecular Chaperones - genetics | Recombinant Proteins - genetics | Chromosomes, Plant - metabolism | DNA Transposable Elements | Protein Interaction Mapping | Plant Proteins - genetics | Ribulose-Bisphosphate Carboxylase - metabolism | Sequence Alignment | Escherichia coli - genetics | Alleles | Holoenzymes - genetics | Chromosomes, Plant - genetics | Chloroplast Proteins - metabolism | Oxidases | Phosphatases | Phytochemistry | Physiological aspects | Research | Health aspects | Carboxylases
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3. Full Text Quantification of growth–defense trade‐offs in a common currency: nitrogen required for phenolamide biosynthesis is not derived from ribulose‐1,5‐bisphosphate carboxylase/oxygenase turnover
by Ullmann‐Zeunert, Lynn and Stanton, Mariana A and Wielsch, Nathalie and Bartram, Stefan and Hummert, Christian and Svatoš, Aleš and Baldwin, Ian T and Groten, Karin
The Plant Journal, ISSN 0960-7412, 08/2013, Volume 75, Issue 3, pp. 417 - 429
Induced defenses are thought to be economical: growth and fitness‐limiting resources are only invested into defenses when needed. To date, this putative... 
Nicotiana attenuata | transcription factor | nicotine | R2R3 | MYB | Manduca sexta | caffeoyl‐putrescine | dicaffeoyl‐spermidine | ribulose‐1,5‐bisphosphate carboxylase/oxygenase | total soluble protein | R2R3-MYB transcription factor | dicaffeoyl-spermidine | ribulose-1,5-bisphosphate carboxylase/oxygenase | caffeoyl-putrescine | MOLECULAR-INTERACTIONS | oxygenase | 5-bisphosphate carboxylase | SIMULATED HERBIVORY | PROTEINASE-INHIBITOR PRODUCTION | HOST NICOTIANA-ATTENUATA | INDUCED PLANT DEFENSES | ribulose-1 | SYSTEMIC DEFENSE | TRANSCRIPTIONAL RESPONSES | PLANT SCIENCES | SPECIALIST LEPIDOPTERAN | MANDUCA-SEXTA LEPIDOPTERA | FITNESS COSTS | Nitrogen - metabolism | Herbivory | Manduca | Tobacco - growth & development | Oxylipins - metabolism | Plant Proteins - genetics | Ribulose-Bisphosphate Carboxylase - metabolism | Pentoses | Animals | Nicotine - metabolism | Plants, Genetically Modified | Cyclopentanes - metabolism | Plant Proteins - metabolism | Tobacco - physiology | Proteins | Defense industry | Metabolites | Growth | Analysis | Physiological aspects | Genetic engineering | Polyamines | Sugars | Monosaccharides | Plant biology | Biosynthesis | Plant growth | Nitrogen | Plant resistance | ribulose-1,5-bisphosphate carboxylase | IRMS | LC-MSE
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4. Full Text Structure of Rubisco from Arabidopsis thaliana in complex with 2‐carboxyarabinitol‐1,5‐bisphosphate
by Valegård, Karin and Hasse, Dirk and Andersson, Inger and Gunn, Laura H
Acta Crystallographica Section D, ISSN 2059-7983, 01/2018, Volume 74, Issue 1, pp. 1 - 9
The crystal structure of ribulose‐1,5‐bisphosphate carboxylase/oxygenase (Rubisco) from Arabidopsis thaliana is reported at 1.5 Å resolution. In light of the... 
Arabidopsis thaliana | rbcS | merohedral twinning | Rubisco | isoforms | ribulose‐1,5‐bisphosphate carboxylase/oxygenase | 2‐carboxyarabinitol‐1,5‐bisphosphate | multigene family | carbon fixation | ribulose-1,5-bisphosphate carboxylase/oxygenase | 2-carboxy arabinitol-1,5-bisphosphate | rbcS multigene family | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CRYSTALLOGRAPHY | ribulose-1 | 2-carboxyarabinitol-1 | BIOPHYSICS | 5-bisphosphate carboxylase/oxygenase | 5-bisphosphate | Pentosephosphates - chemistry | Ribulose-Bisphosphate Carboxylase - chemistry | Ribulose-Bisphosphate Carboxylase - metabolism | Arabidopsis - enzymology | Sugar Alcohols - metabolism | Sugar Alcohols - chemistry | Models, Molecular | Crystallography, X-Ray | Protein Conformation | Pentosephosphates - metabolism | Oxygenase | Genotype & phenotype | Ribulose-1,5-bisphosphate | Coding | Crystals | Isoforms | Ribulose-bisphosphate carboxylase | Catalysis | Plant populations | Photosynthesis | Crystal structure
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5. Full Text Structure of a hyperthermostable dimeric archaeal Rubisco from Hyperthermus butylicus
by Bundela, Rudranuj and Keown, Jeremy and Watkin, Serena and Pearce, Frederick Grant
Acta Crystallographica Section D, ISSN 2059-7983, 06/2019, Volume 75, Issue 6, pp. 536 - 544
The crystal structure of ribulose‐1,5‐bisphosphate carboxylase/oxygenase (Rubisco) from the hyperthermophilic archaeon Hyperthermus butylicus is presented at... 
Rubisco | oligomerization | Hyperthermus butylicus | ribulose‐1,5‐bisphosphate carboxylase oxygenase | thermostability | Thermostability | Oligomerization | Ribulose-1,5-bisphosphate carboxylase oxygenase | MACROMOLECULES | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | 5-bisphosphate carboxylase oxygenase | RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE RUBISCO | RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | BIOCHEMICAL RESEARCH METHODS | CRYSTALLOGRAPHY | ribulose-1 | EVOLUTION | BIOPHYSICS | BISPHOSPHATE CARBOXYLASE/OXYGENASE | QUATERNARY STRUCTURE | PROTEINS | SCATTERING | Oxygenase | Enzymes | Denaturation | Ribulose-bisphosphate carboxylase | Thermal denaturation | Dimers | Electrostatic properties | Thermal stability | Crystal structure
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6. Full Text Function, Structure, and Evolution of the RubisCO-Like Proteins and Their RubisCO Homologs
by F. Robert Tabita and Thomas E. Hanson and Huiying Li and Sriram Satagopan and Jaya Singh and Sum Chan
Microbiology and Molecular Biology Reviews, ISSN 1092-2172, 12/2007, Volume 71, Issue 4, pp. 576 - 599
Article Usage Stats Services MMBR Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | 1,5-DIPHOSPHATE CARBOXYLASE | PHOTOSYNTHETIC RUBISCO | BISPHOSPHATE CARBOXYLASE/OXYGENASE | SULFUR METABOLISM | RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | RHODOSPIRILLUM-RUBRUM | MICROBIOLOGY | LARGE-SUBUNIT GENES | CHLOROBIUM-TEPIDUM | OSTREOCOCCUS-TAURI | Amino Acid Sequence | Ribulose-Bisphosphate Carboxylase - chemistry | Carbon Dioxide - metabolism | Methionine - metabolism | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Ribulose-Bisphosphate Carboxylase - genetics | Models, Molecular | Molecular Sequence Data | Structure-Activity Relationship | Biological Evolution | Ribulose-Bisphosphate Carboxylase - metabolism | Sequence Alignment | Bacteria - enzymology | Bacterial Proteins - metabolism | Catalysis | Sulfur bacteria | Methionine | Physiological aspects | Oxidation-reduction reaction | Rubisco | Research | Chemical properties | Proteins | Chemical reactions | Organisms | Microbiology | Metabolism | Reviews
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7. Full Text Catalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies
by Pearce, F. Grant
Biochemical Journal, ISSN 0264-6021, 11/2006, Volume 399, Issue 3, pp. 525 - 534
During catalysis, all Rubisco (D-ribulose-1,5-bisphosphate carboxylase/oxygenase) enzymes produce traces of several by-products. Some of these by-products are... 
D-ribulose-1,5-bisphosphate carboxylase (Rubisco) | Ligand binding | Side reaction | Photosynthesis | Slow-binding inhibition | RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RIBULOSEBISPHOSPHATE CARBOXYLASE | SIDE REACTIONS | side reaction | 1,5-BISPHOSPHATE CARBOXYLASE | photosynthesis | D-ribulose-1,5-bisphosphate | carboxylase (Rubisco) | SLOW INACTIVATION | SMALL SUBUNITS | OXYGENASE | RUBISCO | SITE-DIRECTED MUTANT | ligand binding | slow-binding inhibition | Organophosphates - metabolism | Species Specificity | Sugar Alcohols - metabolism | Bacterial Proteins - chemistry | Rhodophyta - enzymology | Phylogeny | Sugar Alcohols - pharmacology | Pentosephosphates - pharmacology | Plant Proteins - classification | Plant Proteins - chemistry | Plant Proteins - antagonists & inhibitors | Rhodospirillum rubrum - enzymology | Ribulose-Bisphosphate Carboxylase - antagonists & inhibitors | Plant Proteins - metabolism | Catalysis | Pentosephosphates - metabolism | Binding Sites | Plant Proteins - isolation & purification | Pyruvates - metabolism | Bacterial Proteins - antagonists & inhibitors | Ribulose-Bisphosphate Carboxylase - chemistry | Synechococcus - enzymology | Oxidation-Reduction | Ribulose-Bisphosphate Carboxylase - isolation & purification | Ribulosephosphates - metabolism | Ribulose-Bisphosphate Carboxylase - classification | Glyceric Acids - metabolism | Ribulose-Bisphosphate Carboxylase - metabolism | Sugar Phosphates - metabolism | Protein Binding | Bacterial Proteins - metabolism | Ligands | Bacterial Proteins - classification | Bacterial Proteins - isolation & purification | Tobacco - enzymology | Spinacia oleracea - enzymology | P-glycolate, 2-phosphoglycolate | oxygenase | carboxytetritol-P2, 2′-carboxy-D-tetritol 1,5-bisphosphate | pentodiulose-P2, D-glycero-2,3-pentodiulose 1,5-bisphosphate | carboxyarabinitol-P2, 2′-carboxy-D-arabinitol 1,5-bisphosphate | carboxypentitol-P2, unresolved isomeric mixture of carboxyarabinitol-P2 and 2′-carboxy-D-ribitol 1,5-bisphosphate | xylulose-P2, D-xylulose 1,5-bisphosphate | Rubisco, D-ribulose-1,5-bisphosphate carboxylase | P-glycerate, 3-phospho-D-glycerate | carboxyarabinitol-1-P, 2′-carboxy-D-arabinitol 1-phosphate | ribulose-P2, D-ribulose 1,5-bisphosphate
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8. Full Text Biogenesis and Metabolic Maintenance of Rubisco
by Bracher, Andreas and Whitney, Spencer M and Hartl, F. Ulrich and Hayer-Hartl, Manajit
Annual Review of Plant Biology, ISSN 1543-5008, 4/2017, Volume 68, Issue 1, pp. 29 - 60
Ribulose-1,5-bisphosphate carboxylase oxygenase (Rubisco) mediates the fixation of atmospheric CO 2 in photosynthesis by catalyzing the carboxylation of the... 
metabolic repair | Rubisco | Rubisco activase | assembly chaperone | chaperonin | Chaperonin | Assembly chaperone | Metabolic repair | RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | BUNDLE-SHEATH DEFECTIVE2 | CRYSTAL-STRUCTURE | PHOTOSYNTHETIC CARBON ASSIMILATION | PLANT SCIENCES | FORM-I | PROTEIN-QUALITY CONTROL | 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | SMALL-SUBUNIT | CONCENTRATING MECHANISM | RIBULOSE-BISPHOSPHATE CARBOXYLASE | Chaperonins - metabolism | Ribulose-Bisphosphate Carboxylase - chemistry | Ribulose-Bisphosphate Carboxylase - metabolism | Chaperonins - physiology | Molecular Chaperones | Plants - metabolism | Carbon Dioxide - metabolism | Protein Engineering | Chaperonins - chemistry | Ribulose-Bisphosphate Carboxylase - biosynthesis | Photosynthesis | Protein Folding | Bioengineering | Phosphates | Enzymes | Ribulose-1,5-bisphosphate | Carbon dioxide | Ribulose-bisphosphate carboxylase | Biosynthesis | Chaperones | Machinery | Oxygenase | Fixation | Carboxylation | Ligands | Carbon capture and storage | Assembly | Crop yield | Sugar | Structure-function relationships
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9. Full Text Identification of interactions between abscisic acid and ribulose-1,5-bisphosphate carboxylase/oxygenase
by Galka, Marek M and Rajagopalan, Nandhakishore and Buhrow, Leann M and Nelson, Ken M and Switala, Jacek and Cutler, Adrian J and Palmer, David R. J and Loewen, Peter C and Abrams, Suzanne R and Loewen, Michele C
PLoS ONE, ISSN 1932-6203, 07/2015, Volume 10, Issue 7, p. e0133033
Abscisic acid ((+)-ABA) is a phytohormone involved in the modulation of developmental processes and stress responses in plants. A chemical proteomics approach... 
RUBISCO ACTIVITY | ACTIVATION | COMPARTMENTAL DISTRIBUTION | MOLECULAR-STRUCTURE | INTACT LEAVES | CRYSTAL-STRUCTURE | SPINACH | MULTIDISCIPLINARY SCIENCES | RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | PHOSPHATE-BINDING | LARGE SUBUNIT | Amino Acid Sequence | Ribulose-Bisphosphate Carboxylase - chemistry | Ribulose-Bisphosphate Carboxylase - metabolism | Molecular Sequence Data | Protein Binding | Abscisic Acid - metabolism | Binding Sites | Abscisic Acid - chemistry | Arabidopsis - metabolism | Proteins | Arabidopsis thaliana | Analysis | Abscisic acid | Calorimetry | Sugars | Monosaccharides | Protein binding | Ribulose-bisphosphate carboxylase | Biochemistry | Catalytic activity | Crystallography | X-ray crystallography | Docking | Physiology | Spinach | Catalysis | Electron density | Enzymes | Ribulose-1,5-bisphosphate | Titration calorimetry | Substrate inhibition | Carbon | Oxygenase | Chemistry | Acids | Councils | Proteomics | Affinity | Titration | Binding sites | Structural analysis
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10. Full Text Catalysis and regulation in Rubisco
by Inger Andersson
Journal of Experimental Botany, ISSN 0022-0957, 1/2008, Volume 59, Issue 7, pp. 1555 - 1568
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the incorporation of inorganic CO 2 into the organic molecules of life. Rubisco is... 
Enzymes | Molecules | Active sites | Chloroplasts | Carboxylation | SPECIAL ISSUE REVIEW PAPER | Biochemistry | Catalysis | Plants | Physiological regulation | Crystal structure | specificity | Rubisco | Structure-function studies | Carbon fixation | Light-regulation | ACTIVE-SITE | CRYSTAL-STRUCTURE | RIBULOSEBISPHOSPHATE CARBOXYLASE | XYLULOSE 1,5-BISPHOSPHATE | structure-function studies | CHLOROPLAST RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | carbon fixation | PLANT SCIENCES | LARGE-SUBUNIT | light-regulation | CO2/O-2 specificity | 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | RHODOSPIRILLUM-RUBRUM | EPSILON-AMINO GROUP | RIBULOSE-BISPHOSPHATE CARBOXYLASE | Ribulose-Bisphosphate Carboxylase - chemistry | Ribulose-Bisphosphate Carboxylase - metabolism | Ribulose-Bisphosphate Carboxylase - genetics | Models, Molecular | Protein Conformation | Oxygen - metabolism | Biology with specialization in Structural Biology | Biologi med inriktning mot strukturbiologi | Naturvetenskap | Natural Sciences
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