Ribulose-1,5-bisphosphate carboxylase oxygenase

Tapia, O., Andres, J. and Safont, V. S. Enzyme catalysis and transition structures in vacuo. Transition structures for the enolization, carboxylation and oxygenation reactions in ribulose- 1,5-bisphosphate carboxylase/oxygenase enzyme (Rubisco), J.Chem.Soc.Faraday Trans., 90 (1994), 2365-2374... 

Calvin cycle 752 plastids 752 chloroplast 752 amyloplast 752 carbon-fixation reaction 753 ribulose 1,5-bisphosphate 753 3-phosphoglycerate 753 pentose phosphate pathway 753 reductive pentose phosphate pathway 753 C3 plants 754 ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) 754 rubisco activase 757... 

Hartman, F.C. Harpel, M.R. (1994) Structure, function, regulation and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase. Annu. Rev. Biochem. 63, 197-234. 

Figure 3.1 The Calvin-Benson-Bassham (CBB) cycle. , phosphoribulokinase , ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO).

Figure 6.8. The effects of four organic osmolytes, glycerol, sarcosine, glycine betaine, and TMAO on salt-inhibited ribulose-1,5-bisphosphate-carboxylase-oxygenase (RuBisCO) activity of the cyanobacterium Aphanothece halophytica. The enzyme was placed in a solution containing KC1 at a concentration sufficient to inhibit activity by 50%. Then, increasing concentrations of organic osmolytes were added to the assay medium, leading to restoration of activity. (Modified after Incharoensakdi et al., 1986.)...

Moore, Bd., Palmquist, D.E. Seemann, J R. (1 997) Influence of plant growth at high C02 concentrations on leaf content of ribulose-1,5-bisphosphate carboxylase/oxygenase and intracellular distribution of soluble carbohydrates in tobacco, snapdragon, and parsley. Plant Physiology 11 5, 241-248. 

Carboxylation of ribulose-1,5-bisphosphate by ribulose 1,5-bisphosphate carboxylase-oxygenase (Rubisco) with the formation of two molecules of glycerate-3-P. 

The crux of the pathway (Fig. 1) is the carboxylation of ribulose 1,5-bisphos-phate (Rbu-1,5-P2) at the C-2 carbon, giving rise to a short-lived six-carbon intermediate which is cleaved to produce two molecules of 3-phosphoglycerate (3-PGA) (Eqn. 2). This reaction is catalysed by ribulose-1,5-bisphosphate carboxylase oxygenase (rubisco), one of the most abundant proteins on earth. 

CO, Fixation to ribulose-1,5-bisphosphate (C-site car-boxylation) Ribulose-1,5-bisphosphate carboxylase/ oxygenase (mbisco) 3-Phosphoglycerate (2 times) Green plants, chemolrthoautotro- phs Mg Ni (see above)... 

Wawrik, B., Paul,J. H., andTabita, F. R. (2002). Real-time PCR quantification of rbcL (ribulose-1,5-bisphosphate carboxylase/oxygenase) ruRNA in diatoms and pelagophytes. Appl. Environ. Microbiol. 68, 3771-3779. 

Garcia-Perris, C., and Moreno, J. (1994). Oxidative modification and brealidown of ribulose-1,5-bisphosphate carboxylase oxygenase induced in Euglena gracilis by nitrogen starvation. Planta. 193, 208-215. 

Macintyre, H. L., Sharkey, T. D., and Geider, R. J. (1997). Activation and deactivation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) in three marine microalgae. Photosynthesis Res. 51, 93-106. 

Figure 20.3. Structure of Rubisco. The enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) comprises eight large subunits (one shown in red and the others in yellow) and eight small subunits (one shown in blue and the others in white). The active sites he in the large subunits.

H. Suga vara, H. Yamamoto, N. Shibata, T. Inoue, S. Okada, C. Miyake, A. Yokota, and Y. Kai. 1999. Crystal structure of carboxylase reaction-oriented ribulose 1,5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita J. Biol. Chem. 274 15655-15661. (PubMed)... 

Figure 9 A model of the cyanobacterial carbon concentrating mechanism from Synechococcus PCC 7942, a freshwater species. Solid circles represent transporters located on the plasma membrane and interior to the cell wall. Boxes represent the catalyzing enzymes CA, Carbonic Anhydrase RUBISCO, Ribulose 1-5 bisphosphate Carboxylase Oxygenase. The carboxysome is the site of carbon fixation (dark reactions) and the thylakoid is the site of the light reactions of photosynthesis (after Badger et aL, 2002).

Figure 10 A hypothetical model of carbon acquisition in the marine diatom Thalassiosira weissflogii. Solid circles represent transporters. Catalyzing enzymes CA, carbonic anhydrase PEPC, phosphoenol pyruvate carboxylase PEPCK phospoenol pyruvate carboxykinase RUBISCO, Ribulose 1-5 bisphosphate Carboxylase Oxygenase (after...

In plants and some other eukaryotes, pentoses are components of cell wall polysaccharides such as xylans and arabinogalactans. More interestingly, all green forms of life, i. e., those that perform photosynthesis, contain ribulose 1,5-bisphosphate carboxylase/oxygenase (often abbreviated as Rubisco) as the central enzyme involved in carbon dioxide fixation. Consequently, this enzyme has become of interest in numerous genetic engineering projects aimed at the improvement of photosynthesis in agriculturally important plants [4]. 

In those organisms that perform photosynthesis, further phosphorylation of D-ribulose 5-phos-phate into D-ribulose 1,5-diphosphate by phosphoribulokinase represents an important prerequisite in CO2 fixation. As has already been mentioned, the key and extensively studied enzyme involved in this reaction is D-ribulose 1,5-bisphosphate carboxylase/oxygenase. The subfamily divergence in this multigene family has been studied in certain plants of Triticeae and other families [13]. The occurrence of this enzyme in anoxic Archaea is very interesting, since it had to evolve in the absence of molecular oxygen [14]. 

Figure 3-2. Crystals of various proteins from the hyperthermophilic archaeon, Thermococcus kodakaraensis KOD1. A, rod-like crystal of 06-methylguanine-DNA methyltransferase (MGMT) B, plate-like crystal of MGMT C, bar-like crystal of DNA polymerase D, cubic or hexagonal crystals of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco).

Portis, A. 1992. Regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase activity. Arm. Rev. Plant Physiol. Plant Mol. Biol. 43 415-437. 

Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9 A resolution. EMBO J. 5, 3409-3415. 

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