Ribulose-Bisphosphate Carboxylase: 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.Ribulosephosphates: Ribulose substituted by one or more phosphoric acid moieties.Rhodospirillum rubrum: Vibrio- to spiral-shaped phototrophic bacteria found in stagnant water and mud exposed to light.PentosephosphatesCarboxy-Lyases: 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.Sugar Alcohols: 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)Plants: 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.Chloroplasts: 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.Carbon Dioxide: A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.Thiobacillus: 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.Alcaligenes: 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.Photosynthesis: 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)Acetyl-CoA Carboxylase: 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.Cyanobacteria: 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, Toxic: Plants or plant parts which are harmful to man or other animals.Pyruvate Carboxylase: 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.GluconatesPlant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Rhodobacter sphaeroides: Spherical phototrophic bacteria found in mud and stagnant water exposed to light.Kinetics: The rate dynamics in chemical or physical systems.Macromolecular Substances: 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.Magnesium: 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.Phosphoenolpyruvate Carboxylase: 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.Molecular Sequence Data: 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.Tobacco: A plant genus of the family SOLANACEAE. Members contain NICOTINE and other biologically active chemicals; its dried leaves are used for SMOKING.Light: That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.Genes, Bacterial: The functional hereditary units of BACTERIA.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Amino Acid 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.Sugar PhosphatesMolecular Weight: The sum of the weight of all the atoms in a molecule.Spinacia oleracea: A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)Fructosediphosphates: Diphosphoric acid esters of fructose. The fructose-1,6- diphosphate isomer is most prevalent. It is an important intermediate in the glycolysis process.Phosphatidylinositol 4,5-Diphosphate: 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)Carbon-Carbon Ligases: 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.Plasmids: 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.HexosediphosphatesChromatium: 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.Enzyme Activation: 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.Halothiobacillus: A genus of gram-negative, chemolithoautotrophic bacteria in the family Halothiobacillaceae. Several of its species were reclassified to this genus from THIOBACILLUS.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Glyceric AcidsPiscirickettsiaceae: A family of gram-negative bacteria, in the order Thiotrichales.Fabaceae: 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, Medicinal: 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.Cloning, Molecular: 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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Methylmalonyl-CoA Decarboxylase: 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.Escherichia coli: 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.Ligases: 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.Euglena gracilis: A species of fresh-water, flagellated EUKARYOTES in the phylum EUGLENIDA.Chlamydomonas reinhardtii: A species of GREEN ALGAE. Delicate, hairlike appendages arise from the flagellar surface in these organisms.Protein Conformation: 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, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Biotin: 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.Chlamydomonas: A genus GREEN ALGAE in the order VOLVOCIDA. It consists of solitary biflagellated organisms common in fresh water and damp soil.Mutation: 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.Carbon-Nitrogen Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.Rhamnus: 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.Oxygenases: Oxidases that specifically introduce DIOXYGEN-derived oxygen atoms into a variety of organic molecules.Fructose-Bisphosphate Aldolase: 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.Plant Leaves: 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)Phosphatidylinositol Phosphates: Phosphatidylinositols in which one or more alcohol group of the inositol has been substituted with a phosphate group.Flaveria: A plant genus of the family ASTERACEAE that is used for experiments in molecular genetic studies in plant physiology and development.FructosephosphatesEukaryota: 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.Darkness: The absence of light.Fructose-Bisphosphatase: 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.Zea mays: A plant species of the family POACEAE. It is a tall grass grown for its EDIBLE GRAIN, corn, used as food and animal FODDER.Chlorophyll: Porphyrin derivatives containing magnesium that act to convert light energy in photosynthetic organisms.Phosphatidylinositols: 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.Phosphofructokinase-1: 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.Chemoautotrophic Growth: 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)

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 ...
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
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 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 ...
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
Rubisco is central to carbon assimilation and efforts to improve the efficiency and sustainability of crop production have spurred interest in phenotyping Rubisco activity. We tested the hypothesis that microtiter plate-based methods provide comparable results to those obtained with the radiometric assay that measures the incorporation of 14CO2 into 3-phosphoglycerate (3-PGA). Three NADH-linked assays were tested that use alternative coupling enzymes: glyceraldehyde-3-phosphate-dehydrogenase and glycerolphosphate-dehydrogenase (GAPDH-GlyPDH); phosphoenolpyruvate-carboxylase and malate-dehydrogenase (PEPC-MDH); pyruvate-kinase and lactate-dehydrogenase (PK-LDH). To date there has been no thorough evaluation of their reliability by comparison with the 14C-based method. The three NADH-linked assays were used in parallel to estimate (1) the 3-PGA concentration response curve of NADH oxidation, (2) the Michaelis-Menten constant for RuBP, (3) fully active and inhibited Rubisco activities, and (4) ...
Molecular phyl葉緑体rbcL遺伝子に基づく蘚類ギボウシゴケ目の分子系統学的研究ogeny of the Grimmiales (Musci) based on chloroplast rbcL sequences, Hikobia, 14巻, 1号, pp.55-pp. ...
The CO2-fixing enzyme ribulose bisphosphate carboxylase (Rubisco) works most efficiently at high concentrations of CO2. Many organisms have evolved…
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
3rub: Crystal structure of the unactivated form of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco refined at 2.0-A resolution.
Shop Rubisco accumulation factor ELISA Kit, Recombinant Protein and Rubisco accumulation factor Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Rubisco molecules with at least one (and probably only one) plastid-synthesized small subunit (i.e., L8S7SH) were somewhat less stable than L8S8 molecules. The former lost 35S label slowly during the chase period whereas the latter retained it completely (Figure 6). Perhaps the presence of even one His tag is sufficient to destabilize the whole hexadecamer slightly. However, the turnover rate of L8S7SH was slow compared with that of the D1 protein. Although enhanced turnover might contribute to the scarcity of plastid-synthesized small subunits, it cannot by itself completely explain it.. It is possible, however, that the plastid-synthesized small subunits or their precursors might be subject to rapid turnover before assembly into Rubisco. Although unassembled His-tagged small subunits would be isolated by the Ni2+ chelation procedure, such rapid degradation might keep their steady state pool sizes so small that they would escape detection in pulse-labeling experiments (Figure 6). Rapid ...
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 Rubisco
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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 ...
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 ...
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 ...
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 ...
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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!
Seguindo as indicações do Banco de Portugal, a Fujitsu Services disponibiliza junto da banca unidades recicladoras RBU para detecção de contrafacções e verificação da qualidade das notas de Euro
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 ...
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 ...
Miziorko H, Lorimer G (1983). "Ribulose-1,5-bisphosphate carboxylase-oxygenase". Annu Rev Biochem. 52: 507-35. doi:10.1146/ ... Pilkis S, el-Maghrabi M, Claus T (1990). "Fructose-2,6-bisphosphate in control of hepatic gluconeogenesis. From metabolites to ...
"Ribulose-1,5-bisphosphate-carboxylase - rbcL - Lasianthus strigosus". uniprot.org. Retrieved 2014-08-30. "Descriptions and ...
a) is a phylogenetic tree based on ribulose-1, 5-bisphosphate carboxylase large-subunit genes. (b) is a schematic ventral view ...
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: ...
doi:10.1111/j.1574-6968.1989.tb03353.x. Covey, Simon N.; Taylor, Steven C. (1980). "Rapid purification of ribulose 1,5-bis( ... phosphate) carboxylase from Rhodomicrobium vannielii". FEMS Microbiology Letters. 8 (4): 221. doi:10.1111/j.1574-6968.1980. ...
Servaites JC (1990). "Inhibition of ribulose 1,5-bisphosphate carboxylase/oxygenase by 2-carboxyarabinitol-1-phosphate". Plant ...
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 ... and ribulose 1,5-bisphosphate (RuBP) regeneration. This process occurs only when light is available. Plants do not carry out ...
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, ...
Ribulose-1,5-bisphosphate carboxylase oxygenase, better known as RuBisCO,[note 1] is an enzyme that catalyzes the first major ... One of the subunits of ribulose bisphosphate carboxylase (rubisco) is encoded by chloroplast DNA. Rubisco is the critical ... Wildman SG (2002). "Along the trail from fraction I protein to Rubisco (ribulose bisphosphate carboxylase-oxygenase)". Photosyn ... Portis AR, Parry MA (October 2007). "Discoveries in Rubisco (Ribulose 1,5-bisphosphate carboxylase/oxygenase): a historical ...
... 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 ...
ISBN 978-1-908230-01-0 Wawrik, B; Paul, JH; Tabita, FR (2002). "Real-time PCR quantification of rbcL (ribulose-1,5-bisphosphate ... carboxylase/oxygenase) mRNA in diatoms and pelagophytes". Appl. Environ. Microbiol. 68: 3771-3779. doi:10.1128/aem.68.8.3771- ...
Cavanaugh, CM; Abbott, MS; Veenhuis, M (1988). "Immunochemical Localization of Ribulose-1,5-bisphosphate Carboxylase in the ...
... ribulose 1,5-bisphosphate carboxylase/oxygenase and nitrogenase in the unicellular cyanobionts of Ornithocercus spp. ( ...
"Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins ...
The enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase fixes a molecule of carbon dioxide as phosphoglycerate in the Calvin ...
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, ...
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 ...
... sedoheptulose bisphosphatase and ribulose-1,5-bisphosphate carboxylase. During the dark period, if these enzymes were active a ...
The genome contains the gene for the ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) large subunit, while the small ...
5-bisphosphate carboxylase". Nature. 313 (6001): 358-63. Bibcode:1985Natur.313..358V. doi:10.1038/313358a0. PMID 3969146. De ... "Targeting of a foreign protein to chloroplasts by fusion to the transit peptide from the small subunit of ribulose 1, ...
Carboxysomes encapsulate ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and carbonic anhydrase in carbon-fixing ... For example, in carboxysomes, ribulose-1,5-bisphosphate, bicarbonate, and phosphoglycerate must cross the shell, while carbon ...
The rubiscolins are a group of opioid peptides that are formed during digestion of the ribulose bisphosphate 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 ...
Stein JL, Haygood M, Felbeck H. Nucleotide sequence and expression of a deep-sea ribulose-1,5-bisphosphate carboxylase gene ... The gene coding for ribulose-1,5-bisphosphate carboxylase [RuBisCO; 3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1. ... T1 - Nucleotide sequence and expression of a deep-sea ribulose-1,5-bisphosphate carboxylase gene cloned from a chemoautotrophic ... N2 - The gene coding for ribulose-1,5-bisphosphate carboxylase [RuBisCO; 3-phospho-D-glycerate carboxy-lyase (dimerizing), EC ...
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-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 ...
Ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase may refer to: (Ribulose-bisphosphate carboxylase)-lysine N- ... methyltransferase (Fructose-bisphosphate aldolase)-lysine N-methyltransferase. ...
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. ...
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 ...
Ribulose bisphosphate carboxylase/oxygenase (RuBisCO), the initiating enzyme of the Calvin cycle, occurs in nature in two ... It has been previously established that Thiobacillus neapolitanus fixes CO2 by using a form I ribulose bisphosphate carboxylase ... Insertion Mutation of the Form I cbbL Gene Encoding Ribulose Bisphosphate Carboxylase/Oxygenase (RuBisCO) in Thiobacillus ...
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 ...
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 ...