RuBisCO - Knowledge

1975: 2647:. Later identifications found functionally divergent examples dispersed all over bacteria and archaea, as well as transitionary enzymes performing both RLP-type enolase and RuBisCO functions. It is now believed that the current RuBisCO evolved from a dimeric RLP ancestor, acquiring its carboxylase function first before further oligomerizing and then recruiting the small subunit to form the familiar modern enzyme. The small subunit probably first evolved in anaerobic and thermophilic organisms, where it enabled RuBisCO to catalyze its reaction at higher temperatures. In addition to its effect on stabilizing catalysis, it enabled the evolution of higher specificities for CO 2216:. Even without these strong inhibitors, once every several hundred reactions, the normal reactions with carbon dioxide or oxygen are not completed; other inhibitory substrate analogs are still formed in the active site. Once again, RuBisCO activase can promote the release of these analogs from the catalytic sites and maintain the enzyme in a catalytically active form. However, at high temperatures, RuBisCO activase aggregates and can no longer activate RuBisCO. This contributes to the decreased carboxylating capacity observed during heat stress. 422: 2197:(RuBP) binds more strongly to the active sites of RuBisCO when excess carbamate is present, preventing processes from moving forward. In the light, RuBisCO activase promotes the release of the inhibitory (or — in some views — storage) RuBP from the catalytic sites of RuBisCO. Activase is also required in some plants (e.g., tobacco and many beans) because, in darkness, RuBisCO is inhibited (or protected from hydrolysis) by a competitive inhibitor synthesized by these plants, a 2059:. At ambient levels of carbon dioxide and oxygen, the ratio of the reactions is about 4 to 1, which results in a net carbon dioxide fixation of only 3.5. Thus, the inability of the enzyme to prevent the reaction with oxygen greatly reduces the photosynthetic capacity of many plants. Some plants, many algae, and photosynthetic bacteria have overcome this limitation by devising means to increase the concentration of carbon dioxide around the enzyme, including 1821: 392: 2103: 40: 2461:) and the rate at which product is formed. The authors conclude that RuBisCO may actually have evolved to reach a point of 'near-perfection' in many plants (with widely varying substrate availabilities and environmental conditions), reaching a compromise between specificity and reaction rate. It has been also suggested that the oxygenase reaction of RuBisCO prevents CO 2583: 2167:) move out of the thylakoids in response, increasing the concentration of magnesium in the stroma of the chloroplasts. RuBisCO has a high optimal pH (can be >9.0, depending on the magnesium ion concentration) and, thus, becomes "activated" by the introduction of carbon dioxide and magnesium to the active sites as described above. 5947: 2386:

and be a strategy to increase crop yields. Approaches under investigation include transferring RuBisCO genes from one organism into another organism, engineering Rubisco activase from thermophilic cyanobacteria into temperature sensitive plants, increasing the level of expression of RuBisCO subunits,

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intermediate. Carboxylation and hydration have been proposed as either a single concerted step or as two sequential steps. Concerted mechanism is supported by the proximity of the water molecule to C3 of RuBP in multiple crystal structures. Within the spinach structure, other residues are well placed

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of RuBP is the conversion of the keto tautomer of RuBP to an enediol(ate). Enolisation is initiated by deprotonation at C3. The enzyme base in this step has been debated, but the steric constraints observed in crystal structures have made Lys210 the most likely candidate. Specifically, the carbamate

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RuBisCO. To assist with this buffering process, the newly-evolved enzyme was found to have further developed a series of stabilizing mutations. While RuBisCO has always been accumulating new mutations, most of these mutations that have survived have not had significant effects on protein stability.

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by modulating the effect that substitutions within RuBisCO have on enzymatic function. Substitutions that do not have an effect without the small subunit suddenly become beneficial when it is bound. Furthermore, the small subunit enabled the accumulation of substitutions that are only tolerated in

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RuBisCO is usually only active during the day, as ribulose 1,5-bisphosphate is not regenerated in the dark. This is due to the regulation of several other enzymes in the Calvin cycle. In addition, the activity of RuBisCO is coordinated with that of the other enzymes of the Calvin cycle in several

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There currently are very few effective methods for expressing functional plant Rubisco in bacterial hosts for genetic manipulation studies. This is largely due to Rubisco's requirement of complex cellular machinery for its biogenesis and metabolic maintenance including the nuclear-encoded RbcS

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is then coordinated by the His residues of the active site (His300, His302, His335), and is partially neutralized by the coordination of three water molecules and their conversion to OH. This coordination results in an unstable complex, but produces a favorable environment for the binding of

2055:). In this process, two molecules of phosphoglycolate are converted to one molecule of carbon dioxide and one molecule of 3-phosphoglycerate, which can reenter the Calvin cycle. Some of the phosphoglycolate entering this pathway can be retained by plants to produce other molecules such as 2114:

Some enzymes can carry out thousands of chemical reactions each second. However, RuBisCO is slow, fixing only 3-10 carbon dioxide molecules each second per molecule of enzyme. The reaction catalyzed by RuBisCO is, thus, the primary rate-limiting factor of the Calvin cycle during the day.

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PCC7942 (Se7942) were created by replacing the RuBisCO with the large and small subunit genes of the Se7942 enzyme, in combination with either the corresponding Se7942 assembly chaperone, RbcX, or an internal carboxysomal protein, CcmM35. Both mutants had increased

2289:). The use of oxygen as a substrate appears to be a puzzling process, since it seems to throw away captured energy. However, it may be a mechanism for preventing carbohydrate overload during periods of high light flux. This weakness in the enzyme is the cause of 2425:

into plants. This may improve the photosynthetic efficiency of crop plants, although possible negative impacts have yet to be studied. Advances in this area include the replacement of the tobacco enzyme with that of the purple photosynthetic bacterium

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binds to the RuBisCO active site and to another site on the large chain where it can influence transitions between activated and less active conformations of the enzyme. In this way, activation of bacterial RuBisCO might be particularly sensitive to

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A 3d depiction of the activated RuBisCO from spinach in open form with active site accessible. The active site Lys175 residues are marked in pink, and a close-up of the residue is provided to the right for one of the monomers composing the

2472:, a biochemical model of RuBisCO reaction is used as the core module of climate change models. Thus, a correct model of this reaction is essential to the basic understanding of the relations and interactions of environmental models. 5548:

Cho JH, Hwang H, Cho MH, Kwon YK, Jeon JS, Bhoo SH, Hahn TR (July 2008). "The effect of DTT in protein preparations for proteomic analysis: Removal of a highly abundant plant enzyme, ribulose bisphosphate carboxylase/oxygenase".

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When carbon dioxide is the substrate, the product of the carboxylase reaction is an unstable six-carbon phosphorylated intermediate known as 3-keto-2-carboxyarabinitol-1,5-bisphosphate, which decays rapidly into two molecules of

2232:, and, thus, activase activity depends on the ratio of these compounds in the chloroplast stroma. Furthermore, in most plants, the sensitivity of activase to the ratio of ATP/ADP is modified by the stromal reduction/oxidation ( 5699:

Schulz, L; Guo, Z; Zarzycki, J; Steinchen, W; Schuller, JM; Heimerl, T; Prinz, S; Mueller-Cajar, O; Erb, TJ; Hochberg, GKA (2022-10-14). "Evolution of increased complexity and specificity at the dawn of form I Rubiscos".

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Xi J, Wang X, Li S, Zhou X, Yue L, Fan J, Hao D (November 2006). "Polyethylene glycol fractionation improved detection of low-abundant proteins by two-dimensional electrophoresis analysis of plant proteome".

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to ribulose-1,5-bisphosphate during the Calvin cycle. It is also thought to be the single most abundant protein on Earth, so it is noteworthy that one of its subunits is encoded by the chloroplast genome.

2240:. In this manner, the activity of activase and the activation state of RuBisCO can be modulated in response to light intensity and, thus, the rate of formation of the ribulose 1,5-bisphosphate substrate. 2212:. In the light, RuBisCO activase also promotes the release of CA1P from the catalytic sites. After the CA1P is released from RuBisCO, it is rapidly converted to a non-inhibitory form by a light-activated 534:

from each large chain contribute to the binding sites. A total of eight large chains (= four dimers) and eight small chains assemble into a larger complex of about 540,000 Da. In some Pseudomonadota and

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Cellar NA, Kuppannan K, Langhorst ML, Ni W, Xu P, Young SA (January 2008). "Cross species applicability of abundant protein depletion columns for ribulose-1,5-bisphosphate carboxylase/oxygenase".

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Lorimer GH, Miziorko HM (November 1980). "Carbamate formation on the epsilon-amino group of a lysyl residue as the basis for the activation of ribulosebisphosphate carboxylase by CO2 and Mg2+".

1998:-coordinated water molecule and add directly to the enediol. No Michaelis complex is formed in this process. Hydration of this ketone results in an additional hydroxy group on C3, forming a 299:. It emerged approximately four billion years ago in primordial metabolism prior to the presence of oxygen on Earth. It is probably the most abundant enzyme on Earth. In chemical terms, it 3272:

Yoon M, Putterill JJ, Ross GS, Laing WA (April 2001). "Determination of the relative expression levels of rubisco small subunit genes in Arabidopsis by rapid amplification of cDNA ends".

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Rubisco plods along at a mere three molecules per second... To bypass such slothfulness, plants synthesize a gross amount of Rubisco, sometimes up to 50% of their total protein content!

2090:, both caused by "misfires" halfway in the enolisation-carboxylation reaction. In higher plants, this process causes RuBisCO self-inhibition, which can be triggered by saturating CO 5660:"RuBisCO-like proteins as the enolase enzyme in the methionine salvage pathway: functional and evolutionary relationships between RuBisCO-like proteins and photosynthetic RuBisCO" 2115:

Nevertheless, under most conditions, and when light is not otherwise limiting photosynthesis, the speed of RuBisCO responds positively to increasing carbon dioxide concentration.

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The gem-diol intermediate cleaves at the C2-C3 bond to form one molecule of glycerate-3-phosphate and a negatively charged carboxylate. Stereo specific protonation of C2 of this

2699:. Laboratory-based phylogenetic studies have shown that this evolution was constrained by the trade-off between stability and activity brought about by the series of necessary 2485:

as unfolded proteins. Furthermore, sufficient expression and interaction with Rubisco activase are major challenges as well. One successful method for expression of Rubisco in

1974: 2204:(CA1P). CA1P binds tightly to the active site of carbamylated RuBisCO and inhibits catalytic activity to an even greater extent. CA1P has also been shown to keep RuBisCO in a 6092: 3766:

Andersson I, Knight S, Schneider G, Lindqvist Y, Lundqvist T, Brändén CI, Lorimer GH (1989). "Crystal structure of the active site of ribulose-bisphosphate carboxylase".

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at the C2 carbon of RuBP and subsequent bond cleavage between the C3 and C2 carbon, 2 molecules of glycerate-3-phosphate are formed. The conversion involves these steps:

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Krishnan HB, Natarajan SS (December 2009). "A rapid method for depletion of Rubisco from soybean (Glycine max) leaf for proteomic analysis of lower abundance proteins".

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Carboxylation of the 2,3-enediolate results in the intermediate 3-keto-2-carboxyarabinitol-1,5-bisphosphate and Lys334 is positioned to facilitate the addition of the CO

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RuBisCO was preceded by a period in which mutations granted the enzyme increased stability, establishing a buffer to sustain and maintain the mutations required for C

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form of the minimally active RuBisCO, which with its two components provides a combination of oppositely charged domains required for the enzyme's interaction with O

3089:, one of the subunits of ribulose bisphosphate carboxylase (rubisco) is encoded by chloroplast DNA. Rubisco is the critical enzyme that catalyzes the addition of CO 2656:

its presence. Accumulation of such substitutions leads to a strict dependence on the small subunit, which is observed in extant Rubiscos that bind a small subunit.

2411:-like kinetic characteristics have been attained in rice via nuclear transformation. Robust and reliable engineering for yield of RuBisCO and other enzymes in the C 2052: 5383:

Kim ST, Cho KS, Jang YS, Kang KY (June 2001). "Two-dimensional electrophoretic analysis of rice proteins by polyethylene glycol fractionation for protein arrays".

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available to RuBisCO shifts too far towards oxygen. This phenomenon is primarily temperature-dependent: high temperatures can decrease the concentration of CO

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Ogbaga CC, Stepien P, Athar HU, Ashraf M (June 2018). "Engineering Rubisco activase from thermophilic cyanobacteria into high-temperature sensitive plants".

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Due to its high abundance in plants (generally 40% of the total protein content), RuBisCO often impedes analysis of important signaling proteins such as

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at the active site of RuBisCO, carbon fixation by RuBisCO can be enhanced by increasing the carbon dioxide level in the compartment containing RuBisCO (

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Jin SH, Jiang DA, Li XQ, Sun JW (August 2004). "Characteristics of photosynthesis in rice plants transformed with an antisense Rubisco activase gene".

4643:"Isoleucine 309 acts as a C4 catalytic switch that increases ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) carboxylation rate in Flaveria" 6014:"Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita" 6187: 5613: 6211: 6085: 2015:

results in another molecule of glycerate-3-phosphate. This step is thought to be facilitated by Lys175 or potentially the carbamylated Lys210.

1926:, the C- and N- terminal segments of the enzyme must be closed off, allowing the active site to be isolated from the solvent and lowering the 5316: 5283: 4780: 4413: 3324: 3110:"Enhanced translation of a chloroplast-expressed RbcS gene restores small subunit levels and photosynthesis in nuclear RbcS antisense plants" 3082: 1508: 1104: 688: 6294: 3850:

Taylor TC, Andersson I (January 1997). "The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate".

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Portis AR, Parry MA (October 2007). "Discoveries in Rubisco (Ribulose 1,5-bisphosphate carboxylase/oxygenase): a historical perspective".

5971:"Mutagenesis at two distinct phosphate-binding sites unravels their differential roles in regulation of Rubisco activation and catalysis" 4863:

John Andrews T, Whitney SM (June 2003). "Manipulating ribulose bisphosphate carboxylase/oxygenase in the chloroplasts of higher plants".

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Non-carbon-fixing proteins similar to RuBisCO, termed RuBisCO-like proteins (RLPs), are also found in the wild in organisms as common as

6192: 6142: 4439: 2281:). Several times during the evolution of plants, mechanisms have evolved for increasing the level of carbon dioxide in the stroma (see 6216: 6078: 4957:"Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized" 618:) increases in the light. The role of changing pH and magnesium ion levels in the regulation of RuBisCO enzyme activity is discussed 6363: 6177: 4806:"Plastome-encoded bacterial ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) supports photosynthesis and growth in tobacco" 3812:

Hartman FC, Harpel MR (1994). "Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase".

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Back to the future of photosynthesis: Resurrecting billon-year-old enzymes reveals how photosynthesis adapted to the rise of oxygen.

4523:"Improving photosynthesis and yield potential in cereal crops by targeted genetic manipulation: Prospects, progress and challenges" 5601: 3728:

Cleland WW, Andrews TJ, Gutteridge S, Hartman FC, Lorimer GH (April 1998). "Mechanism of Rubisco: The Carbamate as General Base".

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xygenase), but it has also been argued that is should all be in lower case (rubisco), similar to other terms like scuba or laser.

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on plant protein mixtures would result in multiple intense RuBisCO subunit peaks that interfere and hide those of other proteins.

622:. Once the carbamate is formed, His335 finalizes the activation by returning to its initial position through thermal fluctuation. 6207: 6132: 5396: 218: 3066: 2403:

of RuBisCO has been mostly unsuccessful, though mutated forms of the protein have been achieved in tobacco plants with subunit C

6182: 2087: 352: 4330:"Activation of cyanobacterial RuBP-carboxylase/oxygenase is facilitated by inorganic phosphate via two independent mechanisms" 3567:"Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate" 6239: 4122:"2'-carboxy-D-arabitinol 1-phosphate protects ribulose 1, 5-bisphosphate carboxylase/oxygenase against proteolytic breakdown" 2224:

The removal of the inhibitory RuBP, CA1P, and the other inhibitory substrate analogs by activase requires the consumption of

2154: 169: 145: 6519: 4271:"Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform" 1592: 1176: 772: 409:

for enzyme catalysis are shown in color and labeled. Distances of the hydrogen bonding interactions are shown in angstroms.

2391:, and altering RuBisCO genes to increase specificity for carbon dioxide or otherwise increase the rate of carbon fixation. 2446:

fixation rates when measured as carbon molecules per RuBisCO. However, the mutant plants grew more slowly than wild-type.

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by modifying RuBisCO genes in plants to increase catalytic activity and/or decrease oxygenation rates. This could improve

3158:(Rubisco) is the most prevalent enzyme on this planet, accounting for 30–50% of total soluble protein in the chloroplast; 6261: 4369:

Spreitzer RJ, Salvucci ME (2002). "Rubisco: structure, regulatory interactions, and possibilities for a better enzyme".

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to pass by gas exchange through these openings. Evaporation through the upper side of a leaf is prevented by a layer of

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Wildman SG (2002). "Along the trail from Fraction I protein to Rubisco (ribulose bisphosphate carboxylase-oxygenase)".

4702:"Functional incorporation of sorghum small subunit increases the catalytic turnover rate of Rubisco in transgenic rice" 3052: 1978:

A 3D image of the active site of spinach RuBisCO complexed with the inhibitor 2-carboxyarabinitol-1,5-bisphosphate, CO

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oxygen on Lys210 that is not coordinated with the Mg ion deprotonates the C3 carbon of RuBP to form a 2,3-enediolate.

3635:"Plant-like substitutions in the large-subunit carboxy terminus of Chlamydomonas Rubisco increase CO2/O2 specificity" 3887:"Catalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies" 2540:, though these methods are more time-consuming and less efficient when compared to protamine sulfate precipitation. 1875:(distinct from the "activating" carbon dioxide). RuBisCO also catalyses a reaction of ribulose-1,5-bisphosphate and 355:, unlike RuBisCO, only temporarily fixes carbon. Reflecting its importance, RuBisCO is the most abundant protein in 351:, these pathways are relatively small contributors to global carbon fixation compared to that catalyzed by RuBisCO. 6172: 6127: 4073:"Incorporation of carbon from photosynthetic products into 2-carboxyarabinitol-1-phosphate and 2-carboxyarabinitol" 6504: 1962: 6620: 6607: 6594: 6581: 6568: 6555: 6542: 6304: 6276: 6226: 6162: 6115: 2513:, and regulatory proteins found in lower abundance (10-100 molecules per cell) within plants. For example, using 2400: 2376: 2194: 2158: 1918:. These conditions help explain the low turnover rate found in RuBisCO: In order to increase the strength of the 1868: 1528: 708: 579:

operates by driving deprotonation of the Lys210 residue, causing the Lys residue to rotate by 120 degrees to the

344: 308: 6514: 2644: 466:(formerly proteobacteria), the enzyme usually consists of two types of protein subunit, called the large chain ( 163: 6468: 6411: 6328: 6106: 5505:

Agrawal GK, Jwa NS, Rakwal R (February 2009). "Rice proteomics: ending phase I and the beginning of phase II".

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Igamberdiev AU, Lea PJ (February 2006). "Land plants equilibrate O2 and CO2 concentrations in the atmosphere".

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The capitalization of the name has been long debated. It can be capitalized for each letter of the full name (

1580: 1164: 760: 2695:. This was achieved through enhancement of conformational flexibility of the “open-closed” transition in the 2418:

One avenue is to introduce RuBisCO variants with naturally high specificity values such as the ones from the

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Gupta R, Kim ST (2015). "Depletion of RuBisCO Protein Using the Protamine Sulfate Precipitation Method".

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levels, which might cause it to act in a similar way to how RuBisCO activase functions in higher plants.

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cycle was shown to be possible, and it was first achieved in 2019 through a synthetic biology approach.

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closed during the day, which conserves water but prevents the light-independent reactions (a.k.a. the

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solution. Other existing methods for depleting RuBisCO and studying lower abundance proteins include

2506: 2493: 2380: 1521: 1117: 701: 507: 435: 417:, and is followed by three water molecules (red spheres). All other residues are placed in grayscale. 73: 1533: 713: 594:

is first enabled to bind to the active site by the rotation of His335 to an alternate conformation.

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involves the co-expression of multiple chloroplast chaperones, though this has only been shown for

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A recent theory explores the trade-off between the relative specificity (i.e., ability to favour CO

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Ashida H, Saito Y, Nakano T, Tandeau de Marsac N, Sekowska A, Danchin A, Yokota A (19 June 2007).

2028:. This product, also known as 3-phosphoglycerate, can be used to produce larger molecules such as 90: 6406: 6266: 5932: 5881: 5776: 5751:

Sage RF, Sage TL, Kocacinar F (2012). "Photorespiration and the evolution of C4 photosynthesis".

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Figure 16-48 shows a structural model of the active site, including the involvement of magnesium.

3372: 2937: 2805: 2796: 2744:" in reference to Wildman's attempts to create an edible protein supplement from tobacco leaves. 2668: 2375:

Since RuBisCO is often rate-limiting for photosynthesis in plants, it may be possible to improve

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to aid in the hydration step as they are within hydrogen bonding distance of the water molecule.

1849: 430: 368: 360: 4212:"Rubisco activase constrains the photosynthetic potential of leaves at high temperature and CO2" 2293:, such that healthy leaves in bright light may have zero net carbon fixation when the ratio of O 2602:; explanation of what the small subunit probably does (improve CO2/O2 discrimination); maybe a 590:. The close proximity allows for the formation of a covalent bond, resulting in the carbamate. 6647: 6035: 6000: 5924: 5873: 5838: 5768: 5725: 5681: 5574: 5522: 5487: 5452: 5400: 5365: 5322: 5312: 5279: 5253: 5190: 5139: 5090: 5047: 4996: 4937: 4880: 4845: 4776: 4731: 4682: 4615: 4580: 4500: 4386: 4351: 4310: 4251: 4192: 4143: 4102: 4045: 4002: 3959: 3916: 3867: 3829: 3745: 3701: 3666: 3588: 3547: 3489: 3435: 3320: 3289: 3247: 3196: 3149: 3078: 3035: 2986: 2929: 2921: 2893: 2872: 2855: 2845: 2635: 2521: 2514: 1923: 1907: 1896: 1599: 1567: 1183: 1151: 779: 747: 324: 157: 6056: 5303:. Methods in Molecular Biology. Vol. 1295. New York, NY: Humana Press. pp. 225–33. 5208:

Aigner H, Wilson RH, Bracher A, Calisse L, Bhat JY, Hartl FU, Hayer-Hartl M (December 2017).

4469:"Synthetic glycolate metabolism pathways stimulate crop growth and productivity in the field" 4382: 2465:

depletion near its active sites and provides the maintenance of the chloroplast redox state.

6452: 6447: 6421: 6349: 6289: 6025: 5990: 5982: 5916: 5865: 5828: 5818: 5760: 5717: 5671: 5630: 5622: 5566: 5514: 5479: 5444: 5392: 5357: 5304: 5243: 5233: 5180: 5170: 5129: 5082: 5037: 5027: 4986: 4976: 4927: 4919: 4872: 4835: 4825: 4766: 4758: 4721: 4713: 4672: 4662: 4607: 4570: 4534: 4490: 4480: 4378: 4341: 4300: 4290: 4241: 4231: 4182: 4174: 4133: 4092: 4084: 4037: 3994: 3951: 3906: 3898: 3859: 3821: 3783: 3737: 3693: 3656: 3646: 3615: 3578: 3537: 3527: 3479: 3425: 3415: 3353: 3281: 3237: 3227: 3186: 3139: 3129: 3025: 3017: 2976: 2968: 2913: 2786: 2558: 2486: 2458: 2309:: since plant leaves are evaporatively cooled, limited water causes high leaf temperatures. 2290: 2274: 2213: 2198: 2040: 2039:

and 3-phosphoglycerate. Phosphoglycolate is recycled through a sequence of reactions called

2036: 1820: 471: 1559: 1143: 739: 126: 6499: 6483: 6396: 5764: 5248: 5134: 5117: 4163:"Exceptional sensitivity of Rubisco activase to thermal denaturation in vitro and in vivo" 2733: 277: 5602:"Phylogenetics of Seed Plants: An Analysis of Nucleotide Sequences from the Plastid Gene 5472:

Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences

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Please expand the section to include this information. Further details may exist on the

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can lead to useless or inhibitory by-products. Important inhibitory by-products include

1946:. This reaction involves binding of the carboxylate termini of Asp203 and Glu204 to the 269: 61: 6537: 6478: 6119: 6012:

Sugawara H, Yamamoto H, Shibata N, Inoue T, Okada S, Miyake C, et al. (May 1999).

5995: 5970: 5833: 5798: 5185: 5158: 5042: 5015: 4991: 4956: 4932: 4899: 4726: 4701: 4677: 4642: 4495: 4468: 4097: 4072: 3911: 3886: 3661: 3634: 3542: 3511: 3430: 3396:"Structural mechanism of RuBisCO activation by carbamylation of the active site lysine" 3395: 3242: 3215: 3030: 3005: 2981: 2956: 2688: 2566: 2537: 2433: 2306: 2132: 1919: 1872: 584: 561: 536: 463: 285: 281: 273: 201: 4876: 4305: 4270: 4187: 4162: 3583: 3566: 3144: 3109: 2707:

RuBisCO. Moreover, in order to sustain the destabilizing mutations, the evolution to C

2557:, which codes for the large subunit of RuBisCO has been widely used as an appropriate 2180: 181: 6636: 6442: 6401: 6313: 5986: 5737: 4840: 4805: 4346: 4329: 4246: 4211: 4138: 4121: 3971: 3313: 3175:"Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated" 2562: 2525: 1845: 1513: 1109: 693: 611: 527: 452: 304: 176: 5936: 5780: 5600:

Chase MW, Soltis DE, Olmstead RG, Morgan D, Les DH, Mishler BD, et al. (1993).

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Carbamylation of the ε-amino group of Lys210 is stabilized by coordination with the

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Recently, one efficient method for precipitating out RuBisCO involves the usage of

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When molecular oxygen is the substrate, the products of the oxygenase reaction are

1999: 1833: 1555: 1139: 735: 495: 5483: 5159:"Import of Soluble Proteins into Chloroplasts and Potential Regulatory Mechanisms" 4611: 2736:

at a seminar honouring the retirement of the early, prominent RuBisCO researcher,

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mutations on RuBisCO has been sustained by environmental pressures such as low CO

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conformer, decreasing the distance between the nitrogen of Lys and the carbon of

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