A carboxy-lyase that plays a key role in photosynthetic carbon assimilation in the CALVIN-BENSON CYCLE by catalyzing the formation of 3-phosphoglycerate from ribulose 1,5-biphosphate and CARBON DIOXIDE. It can also utilize OXYGEN as a substrate to catalyze the synthesis of 2-phosphoglycolate and 3-phosphoglycerate in a process referred to as photorespiration.
Ribulose substituted by one or more phosphoric acid moieties.
Vibrio- to spiral-shaped phototrophic bacteria found in stagnant water and mud exposed to light.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
Polyhydric alcohols having no more than one hydroxy group attached to each carbon atom. They are formed by the reduction of the carbonyl group of a sugar to a hydroxyl group.(From Dorland, 28th ed)
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.
A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.
A genus of gram-negative, rod-shaped bacteria that derives energy from the oxidation of one or more reduced sulfur compounds. Many former species have been reclassified to other classes of PROTEOBACTERIA.
A genus of gram-negative, aerobic, motile bacteria that occur in water and soil. Some are common inhabitants of the intestinal tract of vertebrates. These bacteria occasionally cause opportunistic infections in humans.
The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001)
A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.
A phylum of oxygenic photosynthetic bacteria comprised of unicellular to multicellular bacteria possessing CHLOROPHYLL a and carrying out oxygenic PHOTOSYNTHESIS. Cyanobacteria are the only known organisms capable of fixing both CARBON DIOXIDE (in the presence of light) and NITROGEN. Cell morphology can include nitrogen-fixing heterocysts and/or resting cells called akinetes. Formerly called blue-green algae, cyanobacteria were traditionally treated as ALGAE.
Plants or plant parts which are harmful to man or other animals.
A biotin-dependent enzyme belonging to the ligase family that catalyzes the addition of CARBON DIOXIDE to pyruvate. It is occurs in both plants and animals. Deficiency of this enzyme causes severe psychomotor retardation and ACIDOSIS, LACTIC in infants. EC 6.4.1.1.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Spherical phototrophic bacteria found in mud and stagnant water exposed to light.
The rate dynamics in chemical or physical systems.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
An enzyme with high affinity for carbon dioxide. It catalyzes irreversibly the formation of oxaloacetate from phosphoenolpyruvate and carbon dioxide. This fixation of carbon dioxide in several bacteria and some plants is the first step in the biosynthesis of glucose. EC 4.1.1.31.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A plant genus of the family SOLANACEAE. Members contain NICOTINE and other biologically active chemicals; its dried leaves are used for SMOKING.
That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.
The functional hereditary units of BACTERIA.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The sum of the weight of all the atoms in a molecule.
A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)
Diphosphoric acid esters of fructose. The fructose-1,6- diphosphate isomer is most prevalent. It is an important intermediate in the glycolysis process.
A phosphoinositide present in all eukaryotic cells, particularly in the plasma membrane. It is the major substrate for receptor-stimulated phosphoinositidase C, with the consequent formation of inositol 1,4,5-triphosphate and diacylglycerol, and probably also for receptor-stimulated inositol phospholipid 3-kinase. (Kendrew, The Encyclopedia of Molecular Biology, 1994)
Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are the carboxylating enzymes and are mostly biotinyl-proteins. EC 6.4.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
A genus of gram-negative, ovoid to rod-shaped bacteria that is phototrophic. All species use ammonia as a nitrogen source. Some strains are found only in sulfide-containing freshwater habitats exposed to light while others may occur in marine, estuarine, and freshwater environments.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
A genus of gram-negative, chemolithoautotrophic bacteria in the family Halothiobacillaceae. Several of its species were reclassified to this genus from THIOBACILLUS.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
A family of gram-negative bacteria, in the order Thiotrichales.
The large family of plants characterized by pods. Some are edible and some cause LATHYRISM or FAVISM and other forms of poisoning. Other species yield useful materials like gums from ACACIA and various LECTINS like PHYTOHEMAGGLUTININS from PHASEOLUS. Many of them harbor NITROGEN FIXATION bacteria on their roots. Many but not all species of "beans" belong to this family.
Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A carboxy-lyase that catalyzes the decarboxylation of (S)-2-Methyl-3-oxopropanoyl-CoA to propanoyl-CoA. In microorganisms the reaction can be coupled to the vectorial transport of SODIUM ions across the cytoplasmic membrane.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.
A species of fresh-water, flagellated EUKARYOTES in the phylum EUGLENIDA.
A species of GREEN ALGAE. Delicate, hairlike appendages arise from the flagellar surface in these organisms.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A water-soluble, enzyme co-factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk.
A genus GREEN ALGAE in the order VOLVOCIDA. It consists of solitary biflagellated organisms common in fresh water and damp soil.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.
A plant genus of the family RHAMNACEAE. Several species have been reclassified to the FRANGULA genus. It is often called buckthorn but should not be confused with other plants called that.
Oxidases that specifically introduce DIOXYGEN-derived oxygen atoms into a variety of organic molecules.
An enzyme of the lyase class that catalyzes the cleavage of fructose 1,6-biphosphate to form dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The enzyme also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. (Enzyme Nomenclature, 1992) E.C. 4.1.2.13.
Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)
Phosphatidylinositols in which one or more alcohol group of the inositol has been substituted with a phosphate group.
A plant genus of the family ASTERACEAE that is used for experiments in molecular genetic studies in plant physiology and development.
One of the three domains of life (the others being BACTERIA and ARCHAEA), also called Eukarya. These are organisms whose cells are enclosed in membranes and possess a nucleus. They comprise almost all multicellular and many unicellular organisms, and are traditionally divided into groups (sometimes called kingdoms) including ANIMALS; PLANTS; FUNGI; and various algae and other taxa that were previously part of the old kingdom Protista.
The absence of light.
An enzyme that catalyzes the conversion of D-fructose 1,6-bisphosphate and water to D-fructose 6-phosphate and orthophosphate. EC 3.1.3.11.
A plant species of the family POACEAE. It is a tall grass grown for its EDIBLE GRAIN, corn, used as food and animal FODDER.
Porphyrin derivatives containing magnesium that act to convert light energy in photosynthetic organisms.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids.
An allosteric enzyme that regulates glycolysis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-1,6-bisphosphate. D-tagatose- 6-phosphate and sedoheptulose-7-phosphate also are acceptors. UTP, CTP, and ITP also are donors. In human phosphofructokinase-1, three types of subunits have been identified. They are PHOSPHOFRUCTOKINASE-1, MUSCLE TYPE; PHOSPHOFRUCTOKINASE-1, LIVER TYPE; and PHOSPHOFRUCTOKINASE-1, TYPE C; found in platelets, brain, and other tissues.
Growth of organisms using AUTOTROPHIC PROCESSES for obtaining nutrients and chemotrophic processes for obtaining a primary energy supply. Chemotrophic processes are involved in deriving a primary energy supply from exogenous chemical sources. Chemotrophic autotrophs (chemoautotrophs) generally use inorganic chemicals as energy sources and as such are called chemolithoautotrophs. Most chemoautotrophs live in hostile environments, such as deep sea vents. They are mostly BACTERIA and ARCHAEA, and are the primary producers for those ecosystems.

A kinetic study of ribulose bisphosphate carboxylase from the photosynthetic bacterium Rhodospirillum rubrum. (1/1070)

The activation kinetics of purified Rhodospirillum rubrum ribulose bisphosphate carboxylase were analysed. The equilibrium constant for activation by CO(2) was 600 micron and that for activation by Mg2+ was 90 micron, and the second-order activation constant for the reaction of CO(2) with inactive enzyme (k+1) was 0.25 X 10(-3)min-1 . micron-1. The latter value was considerably lower than the k+1 for higher-plant enzyme (7 X 10(-3)-10 X 10(-3)min-1 . micron-1). 6-Phosphogluconate had little effect on the active enzyme, and increased the extent of activation of inactive enzyme. Ribulose bisphosphate also increased the extent of activation and did not inhibit the rate of activation. This effect might have been mediated through a reaction product, 2-phosphoglycolic acid, which also stimulated the extent of activation of the enzyme. The active enzyme had a Km (CO2) of 300 micron-CO2, a Km (ribulose bisphosphate) of 11--18 micron-ribulose bisphosphate and a Vmax. of up to 3 mumol/min per mg of protein. These data are discussed in relation to the proposed model for activation and catalysis of ribulose bisphosphate carboxylase.  (+info)

The localisation of 2-carboxy-D-arabinitol 1-phosphate and inhibition of Rubisco in leaves of Phaseolus vulgaris L. (2/1070)

A recent controversial report suggests that the nocturnal inhibitor of Rubisco, 2-carboxy-D-arabinitol 1-phosphate (CAIP), does not bind to Rubisco in vivo and therefore that CA1P has no physiological relevance to photosynthetic regulation. It is now proved that a direct rapid assay can be used to distinguish between Rubisco-bound and free CA1P, as postulated in the controversial report. Application of this direct assay demonstrates that CA1P is bound to Rubisco in vivo in dark-adapted leaves. Furthermore, CA1P is shown to be in the chloroplasts of mesophyll cells. Thus, CA1P does play a physiological role in the regulation of Rubisco.  (+info)

Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic Archaea. (3/1070)

The predominant pool of organic matter on earth is derived from the biological reduction and assimilation of carbon dioxide gas, catalyzed primarily by the enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO). By virtue of its capacity to use molecular oxygen as an alternative and competing gaseous substrate, the catalytic efficiency of RubisCO and the enzyme's ability to assimilate CO2 may be severely limited, with consequent environmental and agricultural effects. Recent genomic sequencing projects, however, have identified putative RubisCO genes from anoxic Archaea. In the present study, these potential RubisCO sequences, from Methanococcus jannaschii and Archaeoglobus fulgidus, were analyzed in order to ascertain whether such sequences might encode functional proteins. We also report the isolation and properties of recombinant RubisCO using sequences obtained from the obligately anaerobic hyperthermophilic methanogen M. jannaschii. This is the first description of an archaeal RubisCO sequence; this study also represents the initial characterization of a RubisCO molecule that has evolved in the absence of molecular oxygen. The enzyme was shown to be a homodimer whose deduced sequence, along with other recently obtained archaeal RubisCO sequences, differs substantially from those of known RubisCO molecules. The recombinant M. jannaschii enzyme has a somewhat low, but reasonable kcat, however, unlike previously isolated RubisCO molecules, this enzyme is very oxygen sensitive yet it is stable to hyperthermal temperatures and catalyzes the formation of the expected carboxylation product. Despite inhibition by oxygen, this unusual RubisCO still catalyzes a weak yet demonstrable oxygenase activity, with perhaps the lowest capacity for CO2/O2 discrimination ever encountered for any RubisCO.  (+info)

Subfamily divergence in the multigene family of ribulose-1,5-bisphosphate carboxylase/oxygenase (rbcS) in Triticeae and its relatives. (4/1070)

To investigate genetic mechanisms acting on multigene family in plants, we analyzed sequence variation in the rbcS gene of 13 species of Triticeae and one species each of related tribes (Bromeae and Aveneae). A total of 36 rbcS genes were analyzed. Based on dimorphism in the length of intron, the rbcSs of investigated species were classified into two subfamilies A and B. The difference in intron length was caused by an indel of about 200 bp in the middle of the intron. The two subfamilies of rbcS were present in the three tribes, indicating that the divergence of rbcS subfamilies occurred before the split of these tribes. Generally, variation between the two subfamilies of rbcS was larger than that within subfamily, but these two measures were about the same at the tribe level. This result suggested that divergence of the subfamilies of rbcS occurred at about the same time of tribe diversification. The level of nucleotide variation in the exon region between subfamilies was reduced in the Triticeae, but clear change was not detected in the intron sequence. This result suggested that the exon sequences between subfamilies of rbcS were homogenized without affecting the intron sequence in the Triticeae lineage.  (+info)

The stromal protein large subunit of ribulose-1,5-bisphosphate carboxylase is translated by membrane-bound ribosomes. (5/1070)

Translation of the large subunit of ribulose-1,5-bisphosphate carboxylase (LSU) was investigated by labeling of isolated barley plastids with [35S]-methionine. In both chloroplasts and etioplasts, labeling of LSU was severely impaired if plastid membranes were removed from the reaction mixtures. Removal of membrane-bound polysomes with high salt or puromycin greatly decreased translation of LSU. Pulse-labeled chloroplast membranes were shown to release LSU if chased with unlabeled methionine in the presence of stroma. Immunoprecipitation detected higher amounts of labeled LSU translation intermediates associated with the membrane fraction than in the soluble fraction. We therefore conclude that, in plastids, membrane-bound polysomes are required not only for translation of membrane-intrinsic proteins but also for translation of a soluble protein.  (+info)

Chaperonin function: folding by forced unfolding. (6/1070)

The ability of the GroEL chaperonin to unfold a protein trapped in a misfolded condition was detected and studied by hydrogen exchange. The GroEL-induced unfolding of its substrate protein is only partial, requires the complete chaperonin system, and is accomplished within the 13 seconds required for a single system turnover. The binding of nucleoside triphosphate provides the energy for a single unfolding event; multiple turnovers require adenosine triphosphate hydrolysis. The substrate protein is released on each turnover even if it has not yet refolded to the native state. These results suggest that GroEL helps partly folded but blocked proteins to fold by causing them first to partially unfold. The structure of GroEL seems well suited to generate the nonspecific mechanical stretching force required for forceful protein unfolding.  (+info)

Thiomicrospira kuenenii sp. nov. and Thiomicrospira frisia sp. nov., two mesophilic obligately chemolithoautotrophic sulfur-oxidizing bacteria isolated from an intertidal mud flat. (7/1070)

Two new members of the genus Thiomicrospira were isolated from an intertidal mud flat sample with thiosulfate as the electron donor and CO2 as carbon source. On the basis of differences in genotypic and phenotypic characteristics, it is proposed that strain JB-A1T (= DSM 12350T) and strain JB-A2T (= DSM 12351T) are members of two new species, Thiomicrospira kuenenii and Thiomicrospira frisia, respectively. The cells were Gram-negative vibrios or slightly bent rods. Strain JB-A1T was highly motile, whereas strain JB-A2T showed a much lower degree of motility combined with a strong tendency to form aggregates. Both organisms were obligately autotrophic and strictly aerobic. Nitrate was not used as electron acceptor. Chemolithoautotrophic growth was observed with thiosulfate, tetrathionate, sulfur and sulfide. Neither isolate was able to grow heterotrophically. For strain JB-A1T, growth was observed between pH values of 4.0 and 7.5 with an optimum at pH 6.0, whereas for strain JB-A2T, growth was observed between pH 4.2 and 8.5 with an optimum at pH 6.5. The temperature limits for growth were between 3.5 and 42 degrees C and 3.5 and 39 degrees C, respectively. The optimum growth temperature for strain JB-A1T was between 29 and 33.5 degrees C, whereas strain JB-A2T showed optimal growth between 32 and 35 degrees C. The mean maximum growth rate on thiosulfate was 0.35 h-1 for strain JB-A1T and 0.45 h-1 for strain JB-A2T.  (+info)

Thiomicrospira chilensis sp. nov., a mesophilic obligately chemolithoautotrophic sulfuroxidizing bacterium isolated from a Thioploca mat. (8/1070)

A new member of the genus Thiomicrospira, which utilizes thiosulfate as the electron donor and CO2 as the carbon source, was isolated from a sediment sample dominated by the filamentous sulfur bacterium Thioploca. Although the physiological properties investigated are nearly identical to other described species of the genus, it is proposed that strain Ch-1T is a member of a new species, Thiomicrospira chilensis sp. nov., on the basis of differences in genotypic characteristics (16S rRNA sequence, DNA homology, G + C content). Strain Ch-1T was highly motile with a slight tendency to form aggregates in the stationary growth phase. The organism was obligately autotrophic and strictly aerobic. Nitrate was not used as an electron acceptor. Chemolithoautotrophic growth was observed with thiosulfate, tetrathionate, sulfur and sulfide. The isolate was not able to grow heterotrophically. Growth of strain Ch-1T was observed between pH 5.3 and 8.5 with an optimum at pH 7.0. The temperature range for growth was between 3.5 and 42 degrees C; the optimal growth temperature was between 32 and 37 degrees C. The mean maximum growth rate on thiosulfate was 0.4 h-1. This is the second Thiomicrospira species described that has a rod-shaped morphology; therefore discrimination between vibrio-shaped Thiomicrospira and rod-shaped Thiobacilli is no longer valid.  (+info)

Author: Stitt, M. et al.; Genre: Journal Article; Published in Print: 1991; Keywords: flux control (photosynthesis)|br/|nicotiana (transformed with antisense DNA)|br/|ribulose-1,5-bisphosphate carboxylase-oxygenase (control of photosynthesis)|br/|transgenic plant (antisense)|br/|c-3 plants|br/|leaves|br/|limitations|br/|metabolism|br/|phosphate|br/|nitrogen|br/|fixation; Title: Decreased Ribulose-1,5-Bisphosphate Carboxylase-Oxygenase in Transgenic Tobacco Transformed with Antisense Rbcs. 2. Flux-Control Coefficients for Photosynthesis in Varying Light, Co2, and Air Humidity
Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
syc:syc0129_c K01602 ribulose-bisphosphate carboxylase small chain [EC:4.1.1.39] , (GenBank) rbcS; ribulose bisphosphate carboxylase small subunit (A) MSMKTLPKERRFETFSYLPPLSDRQIAAQIEYMIEQGFHPLIEFNEHSNPEEFYWTMWKL PLFDCKSPQQVLDEVRECRSEYGDCYIRVAGFDNIKQCQTVSFIVHRPGRY ...
csg:Cylst_2043 K01602 ribulose-bisphosphate carboxylase small chain [EC:4.1.1.39] , (GenBank) ribulose bisphosphate carboxylase small subunit (A) MQTLPKERRYETLSYLPPLSDAQIAKQIQYILNQGYIPAIEFNETSEPTELYWTMWKLPL FGAKSTQEVLGEVQGCRSQFNNCYIRVVGFDNIKQCQVLSFLVHKPNKY ...
TY - JOUR. T1 - Nucleotide sequence and expression of a deep-sea ribulose-1,5-bisphosphate carboxylase gene cloned from a chemoautotrophic bacterial endosymbiont. AU - Stein, Jeffrey L.. AU - Haygood, Margo. AU - Felbeck, Horst. PY - 1990/11. Y1 - 1990/11. N2 - The gene coding for ribulose-1,5-bisphosphate carboxylase [RuBisCO; 3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39] was cloned from a sulfur-oxidizing chemoautotrophic bacterium that resides as an endosymbiont within the gill tissues of Alvinoconcha hessleri, a gastropod inhabiting deep-sea hydrothermal vents. Nucleotide sequence analysis of the cloned fragment demonstrated that the genes encoding the large (RbcL) and small (RbcS) subunits of the symbiont RuBisCO were organized similarly to the RuBisCO operons of free-living photo- and chemoautotrophic prokaryotes. The symbiont rbcL gene shared the highest degree of nucleotide sequence identity with the cyanobacterium Anabaena (69%) while the rbcS nucleotide sequence shared ...
cbbS; putative ribulose-1,5-bisphosphate carboxylase small subunit protein; K01602 ribulose-bisphosphate carboxylase small chain [EC:4.1.1.39] ...
We describe a highly efficient two-step single-cell reverse transcriptase-polymerase chain reaction technique for analyzing gene expression at the single-cell level. Good reproducibility and a linear dose response indicated that the technique has high specificity and sensitivity for detection and quantification of rare RNA. Actin could be used as an internal standard. The expression of message for Rubisco small subunit (RbcS), chlorophyll a/b-binding protein (Cab), sucrose (Suc):fructan-6-fructosyl transferase (6-SFT), and Actin were measured in individual photosynthetic cells of the barley (Hordeum vulgare) leaf. Only Actin was found in the non-photosynthetic epidermal cells. Cab, RbcS, and 6-SFT genes were expressed at a low level in mesophyll and parenchymatous bundle sheath (BS) cells when sampled from plants held in dark for 40 h. Expression increased considerably after illumination. The amount of 6-SFT, Cab, and RbcS transcript increased more in mesophyll cells than in the parenchymatous ...
TY - JOUR. T1 - Characteristics of ribulose-1,5-bisphosphate carboxylase/oxygenase degradation by lysates of mechanically isolated chloroplasts from wheat leaves. AU - Miyadai, Kenji. AU - Mae, Tadahiko. AU - Makino, Amane. AU - Ojima, Kunihiko. PY - 1990/4. Y1 - 1990/4. N2 - The lysate from intact chloroplasts mechanically isolated from primary leaves of 9 day old seedlings of wheat (Triticum aestivum L. var Aoba) was incubated in the pH range of 5.5 to 8.5 at 37°C for 5 hours. Proteolytic activity against ribulose-1.5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39) was estimated by disappearance of the large subunit of Rubisco or the appearance of its degradation products. Although the activity in lysates was weak, the products were detected by applying Western blotting. The degradation products were similar to those obtained when Rubisco was incubated with the lysate of vacuoles isolated from like leaves. Although some of the products were similar to those from vacuole lysates, ...
K01602 ribulose-bisphosphate carboxylase small chain [EC:4.1.1.39] , (RefSeq) ribulose bisphosphate carboxylase small chain A, chloroplastic- ...
Since RuBisCO is often rate-limiting for photosynthesis in plants, it may be possible to improve photosynthetic efficiency by modifying RuBisCO genes in plants to increase catalytic activity and/or decrease oxygenation rates.[24] This could improve biosequestration of CO2 and be an important climate change strategy. Approaches under investigation include transferring RuBisCO genes from one organism in another organism,engineering Rubisco activase from thermophilic cyanobacteria into temperature sensitive plants, increasing the level of expression of RuBisCO subunits, expressing RuBisCO small chains from the chloroplast DNA, and altering RuBisCO genes to increase specificity for carbon dioxide or otherwise increase the rate of carbon fixation.[25][26]. Although, as the levels of CO2 rise, efforts to increase specificity for CO2 may be unnecessary.. One avenue is to introduce RuBisCO variants with naturally high specificity values such as the ones from the red alga Galdieria partita into plants. ...
Growth at elevated CO2 and temperature often leads to decreased Rubisco activity. We investigated the effects of increased CO2, temperature and nitrogen on the diurnal changes in the control of ribulose-1,5-bisphosphate carboxylase oxygenase (Rubisco) activity in wheat (Triticum aestivum L.). Spring wheat was grown at ambient and 700 μmol mol-1 CO2, under ambient and 4 ºC warmer temperatures, and with two levels of nitrogen supply in field tunnels in a Mediterranean environment. At ear emergence, elevated CO2 increased Rubisco activation, but decreased Rubisco protein and, with high nitrogen, Rubisco specific activity, and had no effect on the rbcS transcript. Warmer temperatures tended to decrease the rbcS mRNA level and Rubisco protein, although the effect on Rubisco activity was small. High nitrogen decreased Rubisco activation or specific activity, depending on the CO2 concentration. It increased Rubisco protein at the end of the night, but accelerated its diurnal loss. The main changes ...
Rubisco. Molecular model of the enzyme rubisco (ribulose bisphosphate carboxylase oxygenase) complexed with 2-carboxyarabinitol biphosphate. Rubisco is thought to be the most abundant and important protein found in nature. It occurs in all plants and fixes carbon dioxide during photosynthesis. - Stock Image F006/9776
Glycine max Ribulose bisphosphate carboxylase small chain 1, chloroplastic (RBCS-1), mRNA; nuclear gene for chloroplast product ...
Rubisco is a major target for improving crop photosynthesis and yield, yet natural diversity in catalytic properties of this enzyme is poorly understood. Rubisco from 25 genotypes of the Triticeae tribe, including wild relatives of bread wheat (Triticum aestivum), were surveyed to identify superior enzymes for improving photosynthesis in this crop. In vitro Rubisco carboxylation velocity (Vc), Michaelis-Menten constants for CO2 (Kc) and O2 (Ko) and specificity factor (Sc/o) were measured at 25 and 35 °C. Vc and Kc correlated positively, while Vc and Sc/o were inversely related. Rubisco large subunit genes (rbcL) were sequenced, and predicted corresponding amino acid differences analysed in relation to the corresponding catalytic properties. The effect of replacing native wheat Rubisco with counterparts from closely related species was analysed by modelling the response of photosynthesis to varying CO2 concentrations. The model predicted that two Rubisco enzymes would increase photosynthetic ...
Photosynthetic carbon fixation in air is constrained by the kinetic properties of Rubisco. Form I Rubisco in higher plants is a large protein (approximately 550 kDa) comprised of eight large (approx. 50-55 kDa) and eight small subunits (approx. 13-18 kDa) to form an L8S8 hexadecamer. Rubisco synthesis and assembly in higher plants is a complex process whereby the large subunit gene (rbcL) is encoded in the chloroplast genome, while the small subunit genes (rbcS) are encoded as a multi-gene family in the nucleus.
The polyadenylation signal of a pea ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit (rbcS) gene has been studied using in vitro mutagenesis and Ti plasmid-mediated transformation of tobacco. Analysis of a mutant that is lacking sequences upstream from -6 (relative to the normal site …
The enzyme at the centre of the fixation of carbon in photosynthesis (which is the ultimate source of our food) is RuBisCO (Ribulose Bisphosphate Carboxylase Oxygenase). It is sometimes called the lazy enzyme because it works so slowly. This is unjust since the process is so difficult that RuBisCO is the only enzyme that can…
Genetic improvement of agronomic crops is necessary to cope with chilling stress. To identify the physiological factors responsible for this genotypic difference in chill-induced inhibition of photosynthesis, leaf CO2 assimilation, the electron flux in the chloroplast and the antioxidant metabolism in isolated chloroplasts were examined in two genotypes of cucumber (Cucumis sativus) plants with distinct chilling tolerance. Cucumber plants were exposed to 100 µmol m-2 s-1 at 9/7°C (day/night) for 10 d and were then returned to optimal conditions for 2 d. Chilling resulted in more significant reductions in rbcL and rbcS transcripts, ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco) content and initial Rubisco activity, leading to higher electron flux to O2 in the chilling-sensitive genotype than in the chilling-tolerant genotype. The chilling-tolerant genotype showed lower H2O2 contents in the chloroplasts by maintaining higher H2O2-scavenging activity in the chloroplasts than in the ...
Biotin carboxylase 1, chloroplastic OS=Populus trichocarpa E-value=7e-87; Biotin carboxylase 2, chloroplastic OS=Populus trichocarpa E-value=3e-86; Biotin carboxylase, chloroplastic OS=Arabidopsis thaliana E-value=2e-83; Biotin carboxylase OS=Nostoc sp. (strain PCC 7120 / UTEX 2576) E-value=3e-65; 2-oxoglutarate carboxylase small subunit OS=Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6) E-value=2e-56 ...
Lineage F.Lineage F is deeply diverging and defined by two highly similar DSR sequences not closely related to any available pure culture sequence. It demonstrates a weak specific association withDesulfotomaculum ruminis by KITCH analysis but forms an independent lineage by all other applied treeing methods.. There is a general need in microbial ecology to more directly relate community structure to community functions. Within the analytical framework of comparative gene sequencing, the most direct linkages are provided by genes encoding key physiological attributes. Several genes have been used in this way, including those for nitrogenase (3, 52-54), [NiFe] hydrogenase (48), ribulose bisphosphate carboxylase/oxygenase (33), methane monooxygenase (30), and ammonia monooxygenase (36, 37). However, with the possible exception of ammonia monooxygenase (restricted to two well-defined lineages within the proteobacteria), none of these genes provide fully comprehensive or consistent coverage. The DSR ...
We investigated whether the reductive pentose phosphate path in guard cells of Pisum sativum had the capacity to contribute significantly to the production of osmotica during stomatal opening in the light. Amounts of ribulose 1,5-bisphophate carboxylase/oxygenase (Rubisco) were determined by the [14C]carboxyarabinitol bisphosphate assay. A guard cell contained about 1.2 and a mesophyll cell about 324 picograms of the enzyme; the ratio was 1:270. The specific activities of Rubisco in guard cells and in mesophyll cells were equal; there was no indication of a specific inhibitor of Rubisco in guard cells. Rubisco activity was 115 femtomol per guard-cell protoplast and hour. This value was different from zero with a probability of 0.99. After exposure of guard-cell protoplasts to 14CO2 for 2 seconds in the light, about one-half of the radioactivity was in phosphorylated compounds and ,10% in malate. Guard cells in epidermal strips produced a different labelling pattern; in the light, ,10% of the ...
Mg2+ in various concentrations was added to purified Rubisco in vitro to gain insight into the mechanism of molecular interactions between Mg2+ and Rubisco. The enzyme activity assays showed that the
FIG. 3. Immunoblot analyses of CbbLS-1, CbbLS-2, and CbbM RubisCOs. CFE (3 μg) were resolved on an SDS-15% polyacrylamide gel and transferred to a polyvinylidene difluoride membrane. An anti-CbbLS-1 oligopeptide antibody (a), an anti-CbbLS-2 oligopeptide antibody (b), and an anti-form II RubisCO antibody raised against CbbM from H. marinus (c) were used. CFE were prepared from 15% (lane 1), 2% (lane 2), 0.15% (lane 3), or 0.03% (lane 4) CO2 cultures. ...
Dr Robert Sharwood, Australian National University Prospects for improving photosynthesis in food and fiber under future climates. The uncertainty of future climate change and the continued reductions in arable land are placing significant pressures on cropping systems to maintain annual increases in productive yield. To mitigate future climates and the increasing threat towards global food security, new solutions to manipulate photosynthesis are required. One crucial enzyme in this process is Rubisco (Ribulose-1,5-bisphosphate carboxylase /oxygenase), which catalyses the rate-limiting step of CO2 fixation of substrate RuBP (ribulose-1,5-bisphosphate carboxylase/oxygenase. The carboxylation of RuBP and the subsequent cycling of the catalytic product 3-phosphoglycerate through the Calvin cycle provides the carbohydrate building blocks for maintaining plant growth and crucial for yield potential. Remarkably, Rubisco is a bifunctional enzyme that often confuses its substrate CO2 with O2 and suffers ...
To understand the effect of heat and drought on three major cereal crops, the physiological and biochemical (i.e., metabolic) factors affecting photosynthesis were examined in rice, wheat, and maize plants grown under long-term water deficit (WD), high temperature (HT) and the combination of both stresses (HT-WD). Diffusional limitations to photosynthesis prevailed under WD for the C3 species, rice and wheat. Conversely, biochemical limitations prevailed under WD for the C4 species, maize, under HT for all three species, and under HT-WD in rice and maize. These biochemical limitations to photosynthesis were associated with Rubisco activity that was highly impaired at HT and under HT-WD in the three species. Decreases in Rubisco activation were unrelated to the amount of Rubisco and Rubisco activase (Rca), but were probably caused by inhibition of Rca activity, as suggested by the mutual decrease and positive correlation between Rubisco activation state and the rate of electron transport. Decreased
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Abstract: Dark CO2 fixation has been shown to rival the importance of oxygenic photosynthesis in the global carbon cycle, especially in stratified environments, such as salt wedge estuaries. We investigated this process in the Columbia River estuary using a variety of techniques including functional gene cloning of cbbL (the large subunit of form I RuBisCO), quantitative real-time PCR (qPCR) estimations of cbbL abundance, and analyses of stimulated 14C-bicarbonate assimilation. A diversity of red-type cbbL genes were retrieved from clone libraries, with 28 unique operational taxonomic units determined from 60 sequences. The majority of the sequences formed two clusters that were distinct from the major clusters typically found in soil environments, revealing the presence of a unique community of autotrophic or facultatively autotrophic/mixotrophic micro-organisms in the Columbia River estuary. qPCR estimates indicated that roughly 0.03-0.15 % of the microbial population harbored the cbbL gene, ...
Recent studies suggest that unidentified prokaryotes fix inorganic carbon at globally significant rates in the immense dark ocean. Using single-cell sorting and whole-genome amplification of prokaryotes from two subtropical gyres, we obtained genomic DNA from 738 cells representing most cosmopolitan lineages. Multiple cells of Deltaproteobacteria cluster SAR324, Gammaproteobacteria clusters ARCTIC96BD-19 and Agg47, and some Oceanospirillales from the lower mesopelagic contained ribulose-1,5-bisphosphate carboxylase-oxygenase and sulfur oxidation genes. These results corroborated community DNA and RNA profiling from diverse geographic regions. The SAR324 genomes also suggested C1 metabolism and a particle-associated life-style. Microautoradiography and fluorescence in situ hybridization confirmed bicarbonate uptake and particle association of SAR324 cells. Our study suggests potential chemolithoautotrophy in several uncultured Proteobacteria lineages that are ubiquitous in the dark oxygenated ...
Many proteins self-assemble to form large supramolecular complexes. Numerous examples of these structures have been characterized, ranging from spherical viruses to tubular protein assemblies. Some new kinds of supramolecular structures are just coming to light, while it is likely there are others that have not yet been discovered. The carboxysome is a subcellular structure that has been known for more than 40 years, but whose structural and functional details are just now emerging. This giant polyhedral body is constructed as a closed shell assembled from several thousand protein subunits. Within this protein shell, the carboxysome encapsulates the CO2-fixing enzymes, Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) and carbonic anhydrase; this arrangement enhances the efficiency of cellular CO2 fixation. The carboxysome is present in many photosynthetic and chemoautotrophic bacteria, and so plays an important role in the global carbon cycle. It also serves as the prototypical member ...
The RNA interference (RNAi) cassette targets the African Cassava Mosaic Virus replication associated gene (AC1) through the production of hairpin RNA (hpRNA). Transcription commences from the A. thaliana Rubisco small subunit 2B promoter and transcribes an inverted repeat of sequences complementary to AC1, before terminating at the Cauliflower Mosaic Virus 35S terminator (CaMV 35 terminator). After transcription, the inverted repeat base pairs to form the hpRNA structure. The hairpin structure is similar to double stranded RNA, which then proceeds to elicit an RNAi response in the host plant. Following processing of the hpRNA, the hosts RNAi proteins target viral transcripts with complementary base pairs to the AC1 inverted repeats. Thus, the RNAi response prevents viral replication and infection via the destruction of AC1, a gene essential for viral replication ...
Carboxysome provides an efficient mechanism for cyanobacteria and chemoautotrophs to fix carbon dioxide (CO_2) and organic metabolites into building blocks of biomolecules. It is a polyhedral body that encapsulates ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), an enzyme that carries out the CO_2 fixation and meanwhile competitively reacts with O_2. Its outer surface is coated by the assembly of thousands of small shell proteins. Many of these shell proteins form oligomeric structures with a semi-permeable 2-3Å radius central pore, suggesting a favorable feature for the binding of anions such as bicarbonate (HCO_3-), the aqueous soluble form of CO_2. The present study examines the translocation HCO_3-, CO_2 and O_2 through the central pores of different isoforms of shell protein complexes from alpha and beta cyanobacteria. We employed umbrella sampling simulations to calculate partitioning free energy profiles of these small molecules and performed detailed electrostatic analysis of ...
In photosynthetic organisms, carbon fixation must be coordinated with the light harvesting reactions to prevent unnecessary energy expenditure in the absence of light. The enzyme phosphoribulokinase (PRK) produces the substrate for the carbon fixation step and switches off reversibly by disulfide bond formation. How this works in β-cyanobacteria is reported in a recent article in Acta Cryst. F by Wilson et al. (2019) and the Proteopedia molecular tour accompanying the article.. The paper describes the dimeric structure of PRK from the cyanobacterium Synechococcus PCC6301. This enzyme catalyzes the transfer of a second phosphate group onto ribulose 5-phosphate, thus creating the ribulose-1,5-bisphosphate (RuBP) substrate for ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO). The need for RuBP is found in virtually all autotrophic organisms, and there are corresponding PRKs in all kingdoms. Phylogenetic analyses of PRKs show two broad classes of enzymes, prokaryotic homo-octameric systems ...
Samples of the intestinal content were collected from the ileum and colon of the Neolithic glacier mummy popularly known as the Tyrolean Iceman, or Ötzi. DNA was extracted from the samples and PCR amplified, using a variety of primer pairs designed to bind to different genes (mammal mitochondrial 12S ribosomal RNA gene, plant/fungal nuclear 18S ribosomal RNA gene, plant chloroplast ribulose bisphosphate carboxylase large subunit gene). This made it possible to distinguish between animal and plant food residues (macroremains) and pollen (microremains). According to the DNA reconstruction, the mans last meal was composed of red deer (Cervus elaphus) meat, and, possibly, cereals; this meal had been preceded by another one based on ibex (Capra ibex), different species of dicots, and cereals. The DNA spectrum corresponding to pollen residues in the colon, on the other hand, fits with the hypothesis that the last journey of the Neolithic hunter/warrior was made through a subalpine coniferous forest ...
Effects of season-long elevated CO2 concentration and temperature on photosynthesis and rubisco activity and amount in field sown ...
Electron microscopy shows the chloroplast to consist of an envelope enclosing a complex of membranes, the thylakoid system often joined or stacked into grana; the lipid membranes, contrast with the background when stained with lipophilic electron dense osmium. The space between the envelope and thylakoid membranes is the chloroplast stroma. The envelope is composed of two membranes each about 5.6 nm thick separated by the intra envelope space (10 nm) with areas of high electron density which are possibly contact points between the membranes; they may be involved in transport, i.e., of proteins between cytosol and stroma. The membranes are lipid bilayers, of galactosyl glycerides and phosphatidyl choline, containing carotenoids but no chlorophyll.. The stroma contains indistinct granules and particles, mainly of proteins; the enzyme ribulose bisphosphate carboxylase (Rubisco) is the major soluble protein and may crystallize in unfavorable conditions such as water stress or air pollution. Other ...
Diatoms are one of the most successful marine eukaryotic algal groups, responsible for up to 20% of the annual global CO2 fixation. The evolution of a CO2-concentrating mechanism (CCM) allowed diatoms to overcome a number of serious constraints on photosynthesis in the marine environment, particularly low [CO2]aq in seawater relative to concentrations required by the CO2 fixing enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO), which is partly due to the slow diffusion rate of CO2 in water and a limited CO2 formation rate from [Formula: see text] in seawater. Diatoms use two alternative strategies to take up dissolved inorganic carbon (DIC) from the environment: one primarily relies on the direct uptake of [Formula: see text] through plasma-membrane type solute carrier (SLC) 4 family [Formula: see text] transporters and the other is more reliant on passive diffusion of CO2 formed by an external carbonic anhydrase (CA). Bicarbonate taken up into the cytoplasm is most likely then ...
DNA barcoding is a way to identify species via their species-specific genetic signatures. To do this for pollen, scientists sequence the DNA from a genetic region known to occur in all plants, but which varies from species to species. There are two parts to the standardized sequence we use for plant DNA barcoding. One is a section of the large subunit of a gene called ribulose-1,5-bisphosphate carboxylase/oxygenase (rbcL for short). The other is a gene called maturase-K (matK). These genes are both essential for a plant to survive, and are thus present in all plants. Once an investigator sequences these gene regions from a sample, they can be compared to a database containing all the known DNA sequences of rbcL and matK to identify the species ...
They noticed something very interesting right away: the carboxysomes in live cells are all lined up, evenly spaced, down the central axis of the rod-shaped bacteria. They hypothesized that there must be something holding the carboxysomes in place, preventing them from diffusing through the cytoplasm. All bacteria have a skeleton, a mesh of proteins that maintains their shape, helps them divide, and can hold chromosomes and other cellular parts in place. When they deleted one of these mesh proteins out of the genome of the photosynthetic bacteria they saw that the cells would become rounder, not able to hold their shape as well, and that the carboxysomes werent evenly spaced any more (figure B). When they knocked out a different skeleton-associated protein, parA, they saw that it seemed to exert special control over the carboxysomes. Deleting this gene allowed the cells to stay rod-shaped, but the carboxysomes werent lined up anymore (figure C).. In the mutants without parA and no even ...
They are initiated by colored pigments, mainly green colored chlorophylls. ... (Dark Reaction) Does not require light Calvin Cycle Occurs in stroma of chloroplast Requires CO2 Uses ATP and NADPH as fuel to … The dark reaction occurs in the stroma of the chloroplast. On the other hand, the dark reactions always take place in the stroma of the chloroplasts. See http://www.merlot.org/merlot/viewMaterial.htm?id=481167, MERLOT description and link to Photosynthesis Interactive Animated Tutorial, which includes an overview to light and dark reactions of photosynthesis, as well as photorespiration. ; Carboxylation occurs with the help of Rubisco enzyme. In contrast, ATP formation through C 2 cycle by re-oxidation of NADH produced in glycine decarboxylase reaction is not an obligatory function, rather an input of energy is necessary to drive the C 2 cycle. Explain that the dark reactions of photosynthesis take place within the stroma. Participants should have some familiarity of plant morphology and ...
This record was replaced or removed. The sequence YP_007084606 is 100% identical to WP_015147336.1 over its full length. Be aware that a NCBI nonredundant RefSeq protein (WP_) can be annotated on large numbers of bacterial genomes that encode that identical protein.. Old YP_007084606.1 New WP_015147336.1 Identical proteins Re-annotation project. ...
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These experiments document that the formation of the enediol(ate) at the active site, though a prerequisite for overall catalysis, is insufficient for completion of the catalytic cycle. These experiments also provide the first direct evidence that the enzyme plays an active, indispensable role in facilitating the attack of COz or O2 on the enediol(ate). Given the Theorell-Chance mechanism of Rubisco, this step could have been viewed as noncatalytic. However, presteady-state kinetics have invoked a partially rate-determining step between the enediol(ate) and its reaction with COz (28), so a direct role of Lys329 in activation of the ene- 46 FRED C. However, this tenet is complicated by the finding based on NMR that the activator within the complex is bicarbonate, not COz (S. Gutteridge and G. H. Lorimer, personal communication). Presumably, bicarbonate engages the sulfhydryl of Cys 191 through H-bonding, which properly juxtaposes the oxyanion as a ligand for Mg2+. If bicarbonate can H-bond with ...
Meet rubisco. You gotta love it. About half of the water-soluble protein in a leaf is rubisco. It is an enzyme that removes carbon dioxide from the air and fixes (attaches) it to other molecules, which will ultimately become sugar. This is the major short-term process that removes carbon dioxide from the air and almost the only process that creates food upon which all the food chains on Earth depend. That is, rubisco is a carboxylase. But it is also an oxygenase. Oxygen molecules can get into rubisco and crowd out the carbon dioxide molecules. This starts a whole cascade of reactions called photorespiration. Rubisco does not react very much with oxygen, but oxygen is over 5000 times as common in the air as carbon dioxide, so it turns out that photorespiration significantly inhibits photosynthesis-by as much as one-quarter. If only rubisco were not such an inefficient carboxylase, the world would be a lot greener-probably over 30 percent greener. Forests would probably grow 30 percent more ...
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Although Mg is abundant within the cell, most is chelated to various organic molecules; only a small fraction of intracellular Mg is in the free (ionized) form, Mgtt Free Mg,SUP,2+,/SUP, regulates manyenzyme activities in cells. The effect of free Mg,SUP,2+,/SUP, concentration on the activities of spinach hloroplast fructose-1, 6-bisphosphatase (FBPase) and ribulose 1, 5-bisphosphate carboxylase (rubisco) was examined. Free Mg,SUP,2+,/SUP, concentrations in the assay mixtures were directly measured by a Mgtsensitive dye, mag-fura-2. FBPase was activated by a physiological concentration range of free Mgt, but the activation of rubisco was not observed. These results suggest that in illuminated chloroplasts, the increase in free Mg,SUP,2+,/SUP, activates FBPase, and this may be a physiological factor to stimulate CO,SUB,2,/SUB, fixation.. ...
The Calvin cycle of photosynthesis begins after light energy is transformed into chemical energy by the cells of plants. The adenosine triphosphate, or ATP, molecules created power the Calvin cycle....
Photosynthesis has two main stages: light reactions and the Calvin cycle; the Calvin cycle has three stages called carbon fixation, reduction and regeneration of RuBP. Photosynthesis is a chemical...
Krauß, Norbert; Hinrichs, W.; Witt, I.; Fromme, P.; Pritzkow, W.; Dauter, Z.; Betzel, C.; Wilson, K.S.; Witt, H.T.; Sänger, W ...
Learn how the Calvin cycle uses the ATP and NADPH formed during the light reactions to generate glucose - fulfilling the ultimate purpose of photosynthesis.
Plants and algae use the enzyme Rubisco to fix carbon dioxide, removing it from the atmosphere and converting it into biomass. However, Rubisco performs this reaction slowly and can also have unwa ...
Easy to read patient leaflet for Activase. Includes indications, proper use, special instructions, precautions, and possible side effects.
Study Flashcards On Micro Bio Photosynthesis at Cram.com. Quickly memorize the terms, phrases and much more. Cram.com makes it easy to get the grade you want!
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If were supposed to have the same amount of Calvin cycle-chemicals before and after, then how many C3 molecules can you make from 48 C1 molecules? If you calculate this, you should be able to get the rest ...
Calvin and Hobbes: The Series is a Fan Fic series co-authored by Swing 123 and garfieldodie. It is perhaps the main installment in what is unofficially …
Miziorko HM, Lorimer GH (1983). "Ribulose-1,5-bisphosphate carboxylase-oxygenase". Annual Review of Biochemistry. 52: 507-35. ... Pilkis SJ, el-Maghrabi MR, Claus TH (June 1990). "Fructose-2,6-bisphosphate in control of hepatic gluconeogenesis. From ...
5-bisphosphate Carboxylase Complexed with Its Substrate, Ribulose- 1,5-bisphosphate*". The Journal of Biological Chemistry. 266 ... "Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red ... Ribulose-1,5-bisphosphate carboxylase-oxygenase, commonly known by the abbreviations RuBisCo, rubisco, RuBPCase, or RuBPco, is ... It can be capitalized for each letter of the full name (Ribulose-1,5 bisphosphate carboxylase/oxygenase), but it has also been ...
The key enzyme is ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO). RuBisCO has been identified in members of the ... The key enzymes of 3-HP and 3-HP/4-HB cycles are acetyl-CoA/propionyl-CoA carboxylase, malonyl-CoA reductase and propionyl-CoA ...
Assembly of newly-synthesised large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts". ... "Synthesis and transport of the small subunit of chloroplast ribulose bisphosphate carboxylase". Nature. 271 (5644): 420. doi: ...
Covey SN, Taylor SC (1980). "Rapid purification of ribulose 1,5-bis(phosphate) carboxylase from Rhodomicrobium vannielii ". ...
5-bisphosphate, the six-carbon intermediate of the ribulose bisphosphate carboxylase reaction". Phil. Trans. R. Soc. Lond. B. ... Portis, Archie; Parry, Martin (2007). "Discoveries in Rubisco (Ribulose 1,5-bisphosphate carboxylase/oxygenase): a historical ... For the Calvin cycle to continue, RuBP (ribulose 1,5-bisphosphate) must be regenerated. So, 5 out of 6 carbons from the 2 G3P ... The three steps involved are: The enzyme RuBisCO catalyses the carboxylation of ribulose-1,5-bisphosphate, RuBP, a 5-carbon ...
Servaites JC (1990). "Inhibition of ribulose 1,5-bisphosphate carboxylase/oxygenase by 2-carboxyarabinitol-1-phosphate". Plant ...
It interacts with large subunit of the ribulose-1,5-bisphosphate carboxylase/oxygenase. CI (~71 kDa) is an RNA helicase with ... It interacts with both the large and small subunits of the ribulose-1,5-bisphosphate carboxylase/oxygenase. The capsid protein ...
5-bisphosphate (RuBP). The enzyme ribulose bisphosphate carboxylase (RuBisCO) carboxylates these RuBP molecules which produces ... TAYLOR, STEPHEN C.; DALTON, HOWARD; DOW, CRAWFORD S. (1981). "Ribulose-1,5-bisphosphate Carboxylase/Oxygenase and Carbon ... Like the RuBP cycle, this cycle begins with 3 molecules of ribulose-5-phosphate. However, instead of phosphorylating ribulose-5 ... First, 3 molecules of ribulose 5-phosphate are phosphorylated to ribulose 1, ...
CS1 maint: discouraged parameter (link) "Ribulose-1,5-bisphosphate-carboxylase - rbcL - Lasianthus strigosus". uniprot.org. ...
... by generating and maintaining a CO2 rich environment around the photosynthetic enzyme ribulose-1,5-bisphosphate carboxylase/ ... Chlamydomonas reinhardtii mutants without ribulose-1, 5-bisphosphate carboxylase-oxygenase lack a detectable pyrenoid. Planta, ...
Tourova, T. P.; Spiridonova, E. M. (2009). "Phylogeny and evolution of the ribulose 1,5-bisphosphate carboxylase/oxygenase ...
The kinetic isotope effect (KIE) of ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCO) is the isotopic fractionation ... Pierce J, Andrews TJ, Lorimer GH (August 1986). "Reaction intermediate partitioning by ribulose-bisphosphate carboxylases with ... all ribulose bisphosphate carboxylases may be nearly perfectly optimized". Proceedings of the National Academy of Sciences of ... doi:10.1016/0014-5793(82)80429-8. Pierce J, Lorimer GH, Reddy GS (1986). "Kinetic mechanism of ribulosebisphosphate carboxylase ...
Kobayashi H., Takabe T., Nishimura M., Akazawa T. Role of the large and small subunits of ribulose-1,5-bisphosphate carboxylase ... Activation and regulation of ribulose bisphosphate carboxylase-oxygenase in the absence of small subunits.. „The Journal of ... Role of the small subunit in ribulose-1,5-bisphosphate carboxylase/oxygenase.. „Archives of biochemistry and biophysics". 2 ( ... Spreitzer R. J.. Questions about the complexity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. „Photosynthesis ...
Along with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCo), phosphoribulokinase is unique to the Calvin Cycle. ... ATP + Mg2+ - D-ribulose 5-phosphate ⇌ {\displaystyle \rightleftharpoons } ADP + D-ribulose 1,5-bisphosphate The two substrates ... I. Phosphoribulokinase and ribulose diphosphate carboxylase". Archives of Biochemistry and Biophysics. 69: 300-10. doi:10.1016/ ... of PRK are ATP and D-ribulose 5-phosphate, whereas its two products are ADP and D-ribulose 1,5-bisphosphate. PRK activity ...
"Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins ... "GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia ...
5-bisphosphate carboxylase/oxygenase) mRNA in diatoms and pelagophytes". Appl. Environ. Microbiol. 68 (8): 3771-3779. doi: ... ISBN 978-1-908230-01-0. Wawrik, B; Paul, JH; Tabita, FR (2002). "Real-time PCR quantification of rbcL (ribulose-1, ...
Cavanaugh, C. M.; Abbott, M. S.; Veenhuis, M. (1988). "Immunochemical localization of ribulose-1,5-bisphosphate carboxylase in ...
... ribulose 1,5-bisphosphate carboxylase/oxygenase and nitrogenase in the unicellular cyanobionts of Ornithocercus spp. ( ...
Cavanaugh, CM; Abbott, MS; Veenhuis, M (1988). "Immunochemical Localization of Ribulose-1,5-bisphosphate Carboxylase in the ...
"Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins ...
To characterize species, the 18S rNA gene, Internal Transcriber Spacer region (ITS), and ribulose-bisphosphate carboxylase gene ...
Carbon isotope fractionation by ribulose 1,5-bisphosphate carboxylase from various organisms (Ph.D.). The University of Texas ... Chase Van Baalen, Patrick Parker, and F. Robert Tabita on her dissertation, titled "Carbon isotope fractionation by ribulose 1, ... Estep, Marilyn F., Tabita, F. Robert, Parker, Patrick L., Van Baalen, Chase (1978). "Carbon Isotope Fractionation by Ribulose-1 ... 5-biphosphate carboxylase from various organisms". While in graduate school, she owned an ice cream truck to help cover ...
This enzyme is ribulose-1,5-bisphosphate carboxylase/oxygenase, abbreviated to RuBisCO, which is responsible for carbon dioxide ... 5-bisphosphate carboxylase". Nature. 287 (5784): 692-697. doi:10.1038/287692a0. Knight, Marc R.; Campbell, Anthony K.; Smith, ... "Molecular cloning and sequencing of cDNA encoding the precursor to the small subunit of chloroplast ribulose-1, ...
The enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) fixes a molecule of carbon dioxide as phosphoglycerate in ... T, Lundqvist; G, Schneider (1991-01-29). "Crystal Structure of the Ternary Complex of ribulose-1,5-bisphosphate Carboxylase, Mg ...
Ribulose-1,5-bisphosphate carboxylase/oxygenase, the enzyme that catalyzes this carboxylation, is possibly the single most ... Many carboxylases, including Acetyl-CoA carboxylase, Methylcrotonyl-CoA carboxylase, Propionyl-CoA carboxylase, and Pyruvate ... OMIM - gamma-glutamyl carboxylase, contributed by McKusick VA, last updated October 2004 [1] Morris DP, Stevens RD, Wright DJ, ... Carboxylation occurs in the liver and is performed by γ-glutamyl carboxylase (GGCX). GGCX requires vitamin K as a cofactor and ...
1983). Structural analysis of nuclear genes coding for the precursor to the small subunit of wheat ribulose-1,5-bisphosphate ... carboxylase. Nature Biotechnology 1: 55-61. Tingey, S. V., et al. (1987). Glutamine synthetase genes of pea encode distinct ...
a) is a phylogenetic tree based on ribulose-1, 5-bisphosphate carboxylase large-subunit genes. (b) is a schematic ventral view ...
... sedoheptulose bisphosphatase and ribulose-1,5-bisphosphate carboxylase. During the dark period, if these enzymes were active a ...
5-bisphosphate carboxylase oxygenase, or RuBisCO. RuBisCO catalyzes the reaction between a five-carbon molecule, ribulose-1,5- ... "Differences in Carbon Isotope Discrimination of Three Variants of D-Ribulose-1,5-bisphosphate Carboxylase/Oxygenase Reflect ... The delta value in the C4 pathway is -12 to -16‰ depleted in 13C due to the combined effects of PEP carboxylase and RuBisCO. ... However, a portion of the isotopically-heavy carbon that is fixed by PEP carboxylase leaks out of the bundle sheath cells. This ...
5-bisphosphate carboxylase/Oxygenase". Plant, Cell and Environment. 27 (9): 1169-1183. doi:10.1111/j.1365-3040.2004.01222.x. ... under natural conditions closely correlates with a reversible heat-dependent reduction of the activation state of ribulose-1, ...
... ribulose-bisphosphate carboxylase)-lysine N-methyltransferase Methylamine-glutamate N-methyltransferase Nicotinamide N- ...
A rise in leaf temperatures may alter ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCo) relationship with carbon ...
5-bisphosphate carboxylase". Nature. 313 (6001): 358-63. Bibcode:1985Natur.313..358V. doi:10.1038/313358a0. PMID 3969146. S2CID ... "Targeting of a foreign protein to chloroplasts by fusion to the transit peptide from the small subunit of ribulose 1, ...
5-bisphosphate carboxylase/oxygenase (also known as RuBisCO), that adds CO2 to ribulose-1,5-bisphosphate (a 5 carbon sugar), to ... The main allosteric activators of PEP carboxylase are acetyl-CoA and fructose-1,6-bisphosphate (F-1,6-BP). Both molecules are ... Phosphoenolpyruvate carboxylase (also known as PEP carboxylase, PEPCase, or PEPC; EC 4.1.1.31, PDB ID: 3ZGE) is an enzyme in ... PEP carboxylase is highly regulated, both by phosphorylation and allostery. The PEP carboxylase enzyme is present in plants and ...
... causing an increase of photorespiration by the oxygenase activity of ribulose-1,5-bisphosphate carboxylase/oxygenase and ... Most (5 out of 6 molecules) of the glyceraldehyde 3-phosphate produced is used to regenerate ribulose 1,5-bisphosphate so the ... A high oxygenase activity, therefore, drains the sugars that are required to recycle ribulose 5-bisphosphate and for the ... such as ribulose bisphosphate (RuBP). Using the ATP and NADPH produced by the light-dependent reactions, the resulting ...
... ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit ... 5-bisphosphate carboxylase-lysine, whereas its two products are S-adenosylhomocysteine and ribulose-1,5-bisphosphate ... ribulose-1,5-bisphosphate carboxylase]-lysine ⇌ {\displaystyle \rightleftharpoons } S-adenosyl-L-homocysteine + [ribulose-1,5- ... In enzymology, a [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase (EC 2.1.1.127) is an enzyme that catalyzes the ...
... is a natural metabolic product of the photorespiration process mediated by the enzyme ribulose 1,5-bisphosphate carboxylase ( ... It uses ribulose 1,5-bisphosphate (RuBP) as substrate and facilitates carboxylation at the C2 carbon via an endiolate ... 7-bisphosphate phosphatase show a significant decrease in the presence of 2-PG. Therefore, degradation of 2-PG during ...
Ribulose-bisphosphate carboxylase)-lysine N-methyltransferase (Fructose-bisphosphate aldolase)-lysine N-methyltransferase This ...
Addition of molecular oxygen to ribulose-1,5-bisphosphate produces 3-phosphoglycerate (PGA) and 2-phosphoglycolate (2PG, or PG ... C4 and CAM photosynthesis both use the enzyme Phosphoenolpyruvate carboxylase (PEPC) to add CO 2 to a 4-Carbon sugar. PEPC is ... CAM plants, such as cacti and succulent plants, also use the enzyme PEP carboxylase to capture carbon dioxide, but only at ... Raven JA, Giordano M, Beardall J, Maberly SC (February 2012). "Algal evolution in relation to atmospheric CO2: carboxylases, ...
Schneider SU, Leible MB, Yang XP (1989). "Strong homology between the small subunit of ribulose-1,5-bisphosphate carboxylase/ ...
... based upon the chloroplast DNA gene ribulose bisphosphate carboxylase large chain (rbcL), found the predilection of several ...
The pyrenoid contains the nuclear-encoded enzyme type II Ribulose-bis-phosphate- carboxylase-oxygenase (Rubisco), which is ...
The irradiation dependence of the compensation point is explained by the RuBP (ribulose-1,5-bisphosphate) concentration. When ... However at low irradiation, only a small fraction of the sites on RuBP carboxylase-oxygenase (RuBisCO) have the electron ...
... observed high activity of ribulose-1,5-bisphosphate carboxylase / oxygenase and ribulose 5-phosphate kinase, the ... It is important to notice that the observed activities of two enzymes, ribulose-1,5-bisphosphate carboxylase / oxygenase and ... ribulose 5-phosphate kinase, are present at high concentrations in the trophosome, but are absent in the muscle. Furthermore, ...
... allowing them to only utilizes ribulose-1,5-bisphosphate carboxylase (Rubisco) to fix CO2 through the Calvin cycle. The enzyme ... This process converts carbon dioxide and ribulose bisphosphate (RuBP, a 5-carbon sugar) into two molecules of 3- ... In specificity, C3 plants does not have PEP carboxylase like C4 plants, ... there's a the low 13C depletion seen in C3 plants compared to C4 plants especially since the C4 pathway uses PEP carboxylase in ...
... ribulose-bisphosphate carboxylase)-lysine N-methyltransferase EC 2.1.1.128: (RS)-norcoclaurine 6-O-methyltransferase EC 2.1. ... 6-bisphosphate synthase EC 2.7.1.107: diacylglycerol kinase EC 2.7.1.108: dolichol kinase EC 2.7.1.109: now EC 2.7.11.31 EC 2.7 ... acetyl-CoA carboxylase) kinase EC 2.7.11.28: tropomyosin kinase EC 2.7.11.29: low-density-lipoprotein receptor kinase EC 2.7. ... 5-bisphosphate phosphokinase EC 2.7.4.24: diphosphoinositol-pentakisphosphate kinase EC 2.7.4.25: (d)CMP kinase EC 2.7.4.26: ...
Other conserved regions in the genomes which are frequently used as marker genes are ribulose-1-5-bisphosphate carboxylase ( ...
... ribulose-bisphosphate carboxylase MeSH D08.811.520.224.125.875 - tyrosine decarboxylase MeSH D08.811.520.224.125.900 - ... acetyl-coa carboxylase MeSH D08.811.464.257.275 - polyketide synthases MeSH D08.811.464.257.500 - pyruvate carboxylase MeSH ... fructose-bisphosphate aldolase MeSH D08.811.520.224.125 - carboxy-lyases MeSH D08.811.520.224.125.050 - adenosylmethionine ... phosphoenolpyruvate carboxylase MeSH D08.811.520.224.125.750 - pyruvate decarboxylase MeSH D08.811.520.224.125.800 - ...
... ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit ... 5-bisphosphate carboxylase-lysine, whereas its two products are S-adenosylhomocysteine and ribulose-1,5-bisphosphate ... ribulose-1,5-bisphosphate carboxylase]-lysine ⇌ {\displaystyle \rightleftharpoons } S-adenosyl-L-homocysteine + [ribulose-1,5- ... In enzymology, a [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase (EC 2.1.1.127) is an enzyme that catalyzes the ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Ribulose bisphosphate carboxylase, type III (IPR017712). Short name: RuBisCO_III Overlapping homologous superfamilies *Ribulose ... Type III ribulose bisphosphate carboxylase (RuBisCO) is composed of a large chain homodimer in a "head-to-tail" conformation. ... Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea.. J. Bacteriol. 185 3049- ...
ribulose 1,5-bisphosphate carboxylase, large subunit [Oscillatoria acuminata PCC 6304]. * This record was replaced or removed. ...
5-bisphosphate carboxylase/oxygenase, Rubisco, plays an important role in photosynthesis as well as in photorespiration. In ... Miziorko, H. M., and Lorimer, G., 1983, Ribulose-1,5-bisphosphate carboxylase-oxygenase, Annu. Rev. Biochem., 52: 507.CrossRef ... Ribulose-1, 5-bisphosphate carboxylase/oxygenase, Rubisco, plays an important role in photosynthesis as well as in ... Knight S., Andersson I., Branden CI., Lorimer G. (1989) Structural Studies of Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase ...
D-ribulose 1,5-bisphosphate + O2 = 2R-3-phosphoglycerate + 2-phosphoglycolate + 2 H+ UniProt ... RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation ...
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) was identified as a putative ABA-binding protein. Radiolabelled- ... and found to be similar to reported and experimentally derived values for the native ribulose-1,5-bisphosphate (RuBP) substrate ... Ribulose-1,5-bisphosphate carboxylase oxygenase Is the Subject Area "Ribulose-1,5-bisphosphate carboxylase oxygenase" ...
RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE. A, B, C, D, E. 444. Thermococcus kodakarensis KOD1. Mutation(s): 0 Gene Names ... Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme of the Calvin-Benson cycle and catalyzes the ... Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme of the Calvin-Benson cycle and catalyzes the ... Ribulose Bisphosphate Carboxylase/oxygenase from Hyperthermophilic Archaeon Pyrococcus kodakaraensis KOD1 is Composed Solely of ...
... the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative ... Ribulose bisphosphate carboxylase large chainUniRule annotation. ,p>Information which has been generated by the UniProtKB ... tr,E8YSE3,E8YSE3_9BURK Ribulose bisphosphate carboxylase large chain OS=Burkholderia sp. CCGE1001 GN=cbbL PE=3 SV=1 ... 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation. ,p>Information which has been ...
Degradation Proteinase Ribulose-1,5-bisphosphate carboxylase Triticum Abbreviations. RuBPCase. ribulose-1,5-bisphosphate ... Degradation of ribulose-1,5-bisphosphate carboxylase by proteolytic enzymes from crude extracts of wheat leaves. ... as determined by measuring the rate of release of amino nitrogen from ribulose-bisphosphate carboxylase (RuBPCase), was found ... Kleinkopf, G.E., Huffaker, R.C., Matheson, A.: A simplified purification and some properties of ribulose 1,5-diphosphate ...
... the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative ... Ribulose bisphosphate carboxylase large chainUniRule annotation. ,p>Information which has been generated by the UniProtKB ... tr,K9WEB9,K9WEB9_9CYAN Ribulose bisphosphate carboxylase large chain OS=Microcoleus sp. PCC 7113 OX=1173027 GN=cbbL PE=3 SV=1 ... 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation. ,p>Information which has been ...
Cloned DNA probes containing genes coding for the large subunit of ribulose-1,5-bisphosphate carboxylase (rbcA) of corn and of ... Isolation and sequence of the gene for the large subunit of ribulose-1,5-bisphosphate carboxylase from the cyanobacterium ... Isolation and sequence of the gene for the large subunit of ribulose-1,5-bisphosphate carboxylase from the cyanobacterium ... Isolation and sequence of the gene for the large subunit of ribulose-1,5-bisphosphate carboxylase from the cyanobacterium ...
Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) catalyzes the initial steps of photosynthetic carbon reduction and ... Ribulose-Bisphosphate Carboxylase/chemistry*. *Ribulose-Bisphosphate Carboxylase/genetics. *Ribulose-Bisphosphate Carboxylase/ ... Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii ... photorespiratory carbon oxidation cycles by combining CO(2) and O(2), respectively, with ribulose-1,5-bisphosphate. Many ...
Ribulose 1,5-Bisphosphate Carboxylase from Autotrophic Micro-organisms DONNA HARRISON; DONNA HARRISON ... DONNA HARRISON, LYNDON J. ROGERS, ARNOLD J. SMITH; Ribulose 1,5-Bisphosphate Carboxylase from Autotrophic Micro-organisms. ...
Photoregulation of expression of genes encoding ribulose-1,5-bisphosphate carboxylase/oxygenase GARETH I. JENKINS GARETH I. ... GARETH I. JENKINS; Photoregulation of expression of genes encoding ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochem Soc ... The carboxylase-large-subunit-binding protein: photoregulation and reversible dissociation Biochem Soc Trans (February,1986) ...
1980) Non-Mendelian mutation affecting ribulose-1,5-bisphosphate carboxylase structure and activity. Nature 285:114-115. ... The Intracellular Localization of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase in Chlamydomonas reinhardtii Olga N. ... 1996) Chlamydomonas reinhardtii mutants without ribulose-1,5-bisphosphate carboxylase-oxygenase lack a detectable pyrenoid. ... 1987) Immunocytochemical localization of ribulose-1,5-bisphosphate carboxylase in the pyrenoid and thylakoid region of the ...
A ribulose 1,5-bisphosphate carboxylase-oxygenase (RubisCO) deletion strain of Rhodospirillum rubrum that was incapable of ... Complementation analysis and regulation of CO2 fixation gene expression in a ribulose 1,5-bisphosphate carboxylase-oxygenase ... Complementation analysis and regulation of CO2 fixation gene expression in a ribulose 1,5-bisphosphate carboxylase-oxygenase ... Complementation analysis and regulation of CO2 fixation gene expression in a ribulose 1,5-bisphosphate carboxylase-oxygenase ...
CO2-Responsive Expression and Gene Organization of Three Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Enzymes and ... CO2-Responsive Expression and Gene Organization of Three Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Enzymes and ... CO2-Responsive Expression and Gene Organization of Three Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Enzymes and ... CO2-Responsive Expression and Gene Organization of Three Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Enzymes and ...
5-bisphosphate carboxylase/oxygenase small subunit (rbcS) gene has been studied using in vitro mutagenesis and Ti plasmid- ... The polyadenylation signal of a pea ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit (rbcS) gene has been studied ... Identification and characterization of cryptic polyadenylation sites in the 3 region of a pea ribulose-1,5-bisphosphate ... carboxylase small subunit gene DNA. 1988 Jun;7(5):329-36. doi: 10.1089/dna.1.1988.7.329. ...
Effects of pH on Activity and Activation of Ribulose 1,5-Bisphosphate Carboxylase at Air Level CO2. Keith A. Mott, Joseph A. ... The effects of pH on catalysis and activation characteristics of spinach ribulose 1,5-bisphosphate (RuBP) carboxylase were ... Effects of pH on Activity and Activation of Ribulose 1,5-Bisphosphate Carboxylase at Air Level CO2 ... Effects of pH on Activity and Activation of Ribulose 1,5-Bisphosphate Carboxylase at Air Level CO2 ...
Diversity of the ribulose bisphosphate carboxylase/oxygenase form I gene (rbcL) in natural phytoplankton communities.. S L ... Diversity of the ribulose bisphosphate carboxylase/oxygenase form I gene (rbcL) in natural phytoplankton communities. ... Diversity of the ribulose bisphosphate carboxylase/oxygenase form I gene (rbcL) in natural phytoplankton communities. ... Diversity of the ribulose bisphosphate carboxylase/oxygenase form I gene (rbcL) in natural phytoplankton communities. ...
Phylogenetic Diversity of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Large-Subunit Genes from Deep-Sea Microorganisms. ... 1999) Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic archaea. J. Bacteriol. 181:1569-1575. ... The genes encoding ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) represent such an enzyme that is involved in ... 1984) Nucleotide sequence of the ribulose bisphosphate carboxylase gene from Rhodospirillum rubrum. Mol. Gen. Genet. 193:220- ...
1985). Crystalline ribulose bisphosphate carboxylase/oxygenase of high integrity and catalytic activity from Nicotiana tabacum ... 1997). Postimport methylation of the small subunit of ribulose-1,5-bisphosphate carboxylase in chloroplasts. FEBS Lett. 408, ... 1994). Relocation of the plastid rbcL gene to the nucleus yields functional ribulose-1,5-bisphosphate carboxylase in tobacco ... 1985). Sequence of a genomic DNA clone for the small subunit of ribulose bisphosphate carboxylase-oxygenase from tobacco. ...
5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1.39) has played a central role in our understanding of chloroplast ... Effect of Mg2+ on the Structure and Function of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase. *Chen Liang, Wu Xiao, +4 ... Alteration of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase activase activities by site-directed mutagenesis.. * ... Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A different perspective. *F Robert Tabita ...
... en_US. ... The isolation, purification, and characterization of ribulose-1, 5-bisphosphate carboxylase/oxygenase from comfrey. K-REx ...
Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) ... Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity ... Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity. Planta, 187 ( ... 5-bisphosphate or CO2 or on Vmax. In contrast replacing a small cassette of residues 338-341 produced a small increase in the ...
Estimating the excess investment in ribulose-1,5-bisphosphate carboxylase/oxygenase in leaves of spring wheat grown under ... The maximal carboxylation rate was proportional to ribulose-1,5-bisphosphate carboxylase/ oxygenase (Rubisco) content, and the ... Estimating the excess investment in ribulose-1,5-bisphosphate carboxylase/oxygenase in leaves of spring wheat grown under ...
Evidence for a conformationally sensitive anion binding site on ribulose -1,5-bisphosphate carboxylase/oxygenase isolated from ... Evidence for a conformationally sensitive anion binding site on ribulose -1,5-bisphosphate carboxylase/oxygenase isolated from ...
  • Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea. (ebi.ac.uk)
  • Other names in common use include rubisco methyltransferase, ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, epsilonN-methyltransferase, S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase, and (dimerizing)]-lysine 6-N-methyltransferase. (wikipedia.org)
  • Ribulose-1, 5-bisphosphate carboxylase/oxygenase, Rubisco, plays an important role in photosynthesis as well as in photorespiration. (springer.com)
  • In addition, Rubisco has an oxygenase activity whereby oxygen is added to ribulose 1, 5-bisphosphate to yield 3-D-phosphoglycerate and 2-phosphoglycolate, the major substrate for photorespiration. (springer.com)
  • The possibility to increase the carboxylase/oxygenase ratio has therefore attracted substantial interest. (springer.com)
  • Is the Subject Area "Ribulose-1,5-bisphosphate carboxylase oxygenase" applicable to this article? (plos.org)
  • Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme of the Calvin-Benson cycle and catalyzes the primary reaction of CO2 fixation in plants, algae, and bacteria. (rcsb.org)
  • Badger, M.R.: The activity and regulation of RuBP Carboxylase-oxygenase. (springer.com)
  • Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyar. (nih.gov)
  • Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5-bisphosphate. (nih.gov)
  • Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) catalyzes the initial steps of photosynthetic carbon reduction and photorespiratory carbon oxidation cycles by combining CO(2) and O(2), respectively, with ribulose-1,5-bisphosphate. (nih.gov)
  • Various studies indicate that ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is present in the pyrenoid, although the fraction of Rubisco localized there remains controversial. (plantphysiol.org)
  • Complementation analysis and regulation of CO2 fixation gene expression in a ribulose 1,5-bisphosphate carboxylase-oxygenase deletion strain of Rhodospirillum rubrum. (asm.org)
  • A ribulose 1,5-bisphosphate carboxylase-oxygenase (RubisCO) deletion strain of Rhodospirillum rubrum that was incapable of photolithoautotrophic growth was constructed. (asm.org)
  • Kinetics and equilibrium binding of the dyes TNS and RH421 to ribulose 1,5 bisphosphate carboxylase/oxygenase (rubisco). (wur.nl)
  • The polyadenylation signal of a pea ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit (rbcS) gene has been studied using in vitro mutagenesis and Ti plasmid-mediated transformation of tobacco. (nih.gov)
  • Diversity of the ribulose bisphosphate carboxylase/oxygenase form I gene (rbcL) in natural phytoplankton communities. (asm.org)
  • They accomplish this task through the action of the Calvin cycle enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO). (asm.org)
  • The phylogenetic diversity of the ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO, E.C. 4.1.1.39) large-subunit genes of deep-sea microorganisms was analyzed. (asm.org)
  • The genes encoding ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) represent such an enzyme that is involved in autotrophy. (asm.org)
  • To assess the extent to which a nuclear gene for a chloroplast protein retained the ability to be expressed in its presumed preendosymbiotic location, we relocated the Rbc S gene for the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) to the tobacco plastid genome. (plantcell.org)
  • The Rbc S gene for the small subunit of the chloroplast photosynthetic enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a much studied example of a gene that has so migrated. (plantcell.org)
  • Alteration of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase activase activities by site-directed mutagenesis. (semanticscholar.org)
  • Plastome engineering of ribulose-1,5-bisphosphate carboxylase/oxygenase in tobacco to form a sunflower large subunit and tobacco small subunit hybrid. (semanticscholar.org)
  • Specificity for activase is changed by a Pro-89 to Arg substitution in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. (semanticscholar.org)
  • Elimination of the Chlamydomonas gene family that encodes the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. (semanticscholar.org)
  • Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) from Anacystis nidulansSynechococcus PCC 6301) was used to generate novel enzymes in Escherichia coli. (lancs.ac.uk)
  • Estimating the excess investment in ribulose-1,5-bisphosphate carboxylase/oxygenase in leaves of spring wheat grown under elevated CO2. (lancs.ac.uk)
  • The maximal carboxylation rate was proportional to ribulose-1,5-bisphosphate carboxylase/ oxygenase (Rubisco) content, and the light-saturated photosynthetic rate at 70 Pa CO2 was proportional to the thylakoid ATP-synthase content. (lancs.ac.uk)
  • Two different forms of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), which catalyzes the carbon fixation step of the Calvin-Benson cycle, may be responsible for the distinction in d 13 C values. (vacets.org)
  • Marine phytoplankton fix carbon dioxide primarily through the action of ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO), the first enzyme in the Calvin Cycle. (usf.edu)
  • Decreased Ribulose-1,5-Bisphosphate Carboxylase-Oxygenase in Transgenic Tobacco Transformed with Antisense Rbcs. (mpg.de)
  • Complete stoichiometry of the reaction catalyzed by ribulose 1,5-bisphosphate (RuBP) oxygenase from spinach and Rhodospirillum rubrum has been determined. (elsevier.com)
  • Results are in excellent accord with the expected stoichiometry for catalysis by RuBP oxygenase and also enable an estimate of competing catalysis by RuBP carboxylase. (elsevier.com)
  • It is catalyzed by the enzyme ribulose bisphosphate carboxylase/oxygenase (abbreviated RubisCO ). (brainkart.com)
  • Ribulose bisphosphate-carboxylase/oxygenase is the only enzyme that enables the fixation of atmospheric CO 2 for the formation of biomass . (brainkart.com)
  • The bacterial enzymes consisting of only two large subunits, however, exhibit a higher ratio of oxygenase versus carboxylase activity than the plant enzymes, which consist of eight large and eight small subunits. (brainkart.com)
  • Marine research has identified five different gene sequences that express the Calvin cycle enzyme ribulose-1,5-biphosphate carboxylase/oxygenase. (readabstracts.com)
  • Diel rhythms in ribulose-1,5-bisphosphate carboxylase/oxygenase and glutamine synthetase gene expression in a natural population of marine picoplanktonic cyanobacteria (Synechococcus spp. (readabstracts.com)
  • This was the conclusion of researchers who discovered temporal and reciprocal oscillations in the production of ribulose bisphosphate carboxylase/oxygenase and glutamine synthetase. (readabstracts.com)
  • These residues are essential to catalysis by the carboxylase activity of ribulose bisphosphate carboxylase/oxygenase. (elsevier.com)
  • Proteolytic activity against ribulose-1.5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39) was estimated by disappearance of the large subunit of Rubisco or the appearance of its degradation products. (elsevier.com)
  • ribulose bisphosphate carboxylase-oxygenase) lub karboksydysmutaza [2] . (wikipedia.org)
  • That's why this is carboxylase/oxygenase. (coursera.org)
  • MISCELLANEOUS: Because the Archaea possessing a type III RuBisCO CC are all anaerobic, it is most likely that only the carboxylase CC activity of RuBisCO, and not the competitive oxygenase activity CC (by which RuBP reacts with O(2) to form one molecule of 3- CC phosphoglycerate and one molecule of 2-phosphoglycolate), is CC biologically relevant in these strains. (genome.jp)
  • It's called ribulose 1,5-bisphosphate carboxylase/oxygenase. (valleyadvocate.com)
  • Ribulose-1,5-bisphosphate carboxylase-oxygenase, commonly known by the abbreviations RuBisCo, rubisco, RuBPCase, or RuBPco, is an enzyme involved in the first major step of carbon fixation, a process by which atmospheric carbon dioxide is converted by plants and other photosynthetic organisms to energy-rich molecules such as glucose. (wikipedia.org)
  • RuBisCo is an abbreviation for Ribulose-1,5-bisphosphate carboxylase/oxygenase. (enn.com)
  • Using both native and reversed TPs for two well-studied precursors, small subunit of ribulose-1,5-bis-phosphate carboxylase/oxygenase, and ferredoxin, we exposed these two modes of recognition. (plantcell.org)
  • In maize, two distinct ribulose 1,5-bisphosphate carboxylase/oxygenase activase transcripts have different day/night patterns of expression. (wikipathways.org)
  • Andersson, I., Taylor, T.C.: Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase. (springer.com)
  • Andrews, T.J., Whitney, S.M.: Manipulating ribulose bisphosphate carboxylase/oxygenase in the chloroplasts of higher plants. (springer.com)
  • Ribulose-1,5-bisphosphate carboxylase oxygenase , better known as RuBisCO , [note 1] is an enzyme that catalyzes the first major step of carbon fixation in the Calvin cycle . (wikipedia.org)
  • Carboxysomes, containing the enzyme ribulose bisphosphate carboxylase/oxygenase, and chlorosomes, sacs of self‐aggregated bacterriochlorophyll are carbon‐fixing and light‐harvesting organelles, respectively. (els.net)
  • Ribulose bisphosphate carboxylase/oxygenase particles clearly visible within the carboxysomes. (els.net)
  • Here, polyhedral shell proteins encase the enzymes carbonic anhydrase and RuBisCo (ribulose-1,5-bisphosphate carboxylase/oxygenase). (biochemj.org)
  • The most widely known examples of this are CO2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. (dur.ac.uk)
  • Enclosed within the carboxysome interior is the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO). (thefreelibrary.com)
  • The carboxysome, a polyhedral protein microcompartment found in all cyanobacteria and in many chemoautotrophs, is filled with ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO), the enzyme that catalyzes the fixation of C[O.sub.2] onto ribulose-1,5-bisphosphate and produces two molecules of 3-phosphoglycerate. (thefreelibrary.com)
  • Type III ribulose bisphosphate carboxylase (RuBisCO) is composed of a large chain homodimer in a "head-to-tail" conformation. (ebi.ac.uk)
  • RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. (rcsb.org)
  • RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. (uniprot.org)
  • In plants, rubisco activase (Rca) regulates rubisco by removing inhibitory molecules such as ribulose‐1,5‐bisphosphate (RuBP). (usda.gov)
  • concentration on the activities of spinach hloroplast fructose-1, 6-bisphosphatase (FBPase) and ribulose 1, 5-bisphosphate carboxylase (rubisco) was examined. (nii.ac.jp)
  • Ribulose-1,5-bisphosphate (RubisCO) was a primary oxidation target. (frontiersin.org)
  • Phosphoenolpyruvate carboxylase, unlike RuBisCO, only temporarily fixes carbon. (wikipedia.org)
  • Substrates for RuBisCO are ribulose-1,5-bisphosphate and carbon dioxide (distinct from the "activating" carbon dioxide). (wikipedia.org)
  • RuBisCO also catalyses a reaction of ribulose-1,5-bisphosphate and molecular oxygen (O 2) instead of carbon dioxide (CO 2). (wikipedia.org)
  • One of the subunits of ribulose bisphosphate carboxylase (rubisco) is encoded by chloroplast DNA . (wikipedia.org)
  • Rubisco is the critical enzyme which catalyzes the addition of CO 2 to ribulose-1,5-bisphosphate during the Calvin cycle (see Figure 2.39). (wikipedia.org)
  • The effects of pH on catalysis and activation characteristics of spinach ribulose 1,5-bisphosphate (RuBP) carboxylase were examined at air level of CO 2 . (plantphysiol.org)
  • Before initiation and after termination, RuBP has been measured either by release of equimolar orthophosphate at 25°C in the presence of 1 n NaOH or by complete carboxylation using 14 CO 2 and RuBP carboxylase. (elsevier.com)
  • The key reaction for photosynthetic CO2 assimilation is the binding of atmospheric CO2 to the acceptor ribulose 1,5-bisphosphate (RuBP) to syn- thesize two molecules of 3-phosphoglycerate. (brainkart.com)
  • Keto-enol isomerization of RuBP yields an enediol, which reacts with CO 2 to form the intermediate 2-carboxy 3-ketoarabinitol 1,5-bisphosphate, which is cleaved to two molecules of 3-phosphoglycerate. (brainkart.com)
  • FUNCTION: Catalyzes the addition of molecular CO(2) and H(2)O to CC ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3- CC phosphoglycerate (3-PGA). (genome.jp)
  • In chemical terms, it catalyzes the carboxylation of ribulose-1,5-bisphosphate (also known as RuBP). (wikipedia.org)
  • Cloned DNA probes containing genes coding for the large subunit of ribulose-1,5-bisphosphate carboxylase ( rbc A) of corn and of Chlamydomonas were used to identify, by heterologous hybridization, DNA fragments from Anabaena 7120 carrying the corresponding gene sequence. (pnas.org)
  • Saluja, AK & McFadden, BA 1980, ' Modification of histidine at the active site of spinach ribulose bisphosphate carboxylase ', Biochemical and Biophysical Research Communications , vol. 94, no. 4, pp. 1091-1097. (elsevier.com)
  • Comparative studies on the activity of carboxylases and other enzymes in relation to the new pathway of photosynthetic carbon dioxide fixation in tropical grasses. (wikipathways.org)
  • For these reasons, the ratio of oxygenation to carboxylation during photosynthesis of a leaf at 25°C is in the range of 1:4 to 1:2 , which implies that every third to fifth ribulose 1,5-bisphosphate molecule is consumed in the side-reaction . (brainkart.com)
  • An enzyme (in Greek en = in and zyme = leaven) is a protein , or protein complex , that catalyzes a chemical reaction and also controls the 3D orientation of the catalyzed substrates. (academickids.com)
  • Regulation of Soybean Net Photosynthetic CO(2) Fixation by the Interaction of CO(2), O(2), and Ribulose 1,5-Diphosphate Carboxylase. (semanticscholar.org)
  • Nucleotide sequence of ribulosebisphosphate carboxylase gene from Rhodospirillum rubrum. (nii.ac.jp)
  • Regulation of Ribulose Bisphosphate Carboxylase Gene Expression in Nat" by S. L. Pichard, L. Campbell et al. (usf.edu)
  • Regulation of Ribulose Bisphosphate Carboxylase Gene Expression in Natural Phytoplankton Communities .1. (usf.edu)
  • E8YSE3_9BURK Ribulose bisphosphate carboxylase large chain OS=Burkholderia sp. (uniprot.org)
  • K9WEB9_9CYAN Ribulose bisphosphate carboxylase large chain OS=Microcoleus sp. (uniprot.org)
  • The enzymatically active substrate (ribulose 1,5-bisphosphate) binding sites are located in the large chains that form dimers in which amino acids from each large chain contribute to the binding sites. (wikipedia.org)
  • Olympic, maximum proteinase activity, as determined by measuring the rate of release of amino nitrogen from ribulose-bisphosphate carboxylase (RuBPCase), was found to be obtained only when EDTA and L-cysteine were included in the extraction buffer. (springer.com)
  • and by higher ribulose-1,5-bisphosphate carboxylase (RuBPC, EC 4.1.1.39) activity compared with other ear elements ( Aliyev, 2012 ). (frontiersin.org)
  • A carboxy-lyase that plays a key role in photosynthetic carbon assimilation in the CALVIN-BENSON CYCLE by catalyzing the formation of 3-phosphoglycerate from ribulose 1,5-biphosphate and CARBON DIOXIDE. (childrensmercy.org)
  • One substrate, ribulose bisphosphate, the product 3-phosphoglycerate and two competitive inhibitors protected against inactivation, thereby indicating that DEP modifies the active site. (elsevier.com)
  • abstract = "Ribulose 1,5-bisphosphate carboxylase from spinach was rapidly inactivated by diethylpyrocarbonate (DEP) at pH 7.0 and 30°C. The inactivation showed saturation kinetics with a half-inactivation time at saturating DEP equal to 0.1 minutes and KDEP = 7.4 mM. (elsevier.com)
  • Our model predicts that ribulose-1,5-bisphosphate (RuBP), the substrate of Rubisco, and 3-phosphoglycerate (3PGA), its product, diffuse in and out of the pyrenoid, respectively, with higher fluxes in CCM-induced cells. (princeton.edu)
  • The first step of this reaction involves the enzyme ribulose bisphosphate carboxylase, abbreviated as rubisco . (fiveable.me)
  • The small subunit of ribulose-bisphosphate carboxylase (Rubisco), encoded by rbcS, is essential for photosynthesis in both C3 and C4 plants, even though the cell specificity of rbcS expression is different between C3 and C4 plants. (sparrho.com)
  • The Calvin cycle starts with fixation of CO2 by ribulose-5-phosphate to form two molecule of 3-phosphoglycerate and ends with regeneration of ribulose. (knowt.io)
  • Increasing the concentration of CO2 is expected to accelerate the carboxylase reaction. (knowt.io)
  • The pathway can be separated into non-oxidative steps in which ribulose-5-phosphate is converted into three 7-carbon sugars. (knowt.io)