4.1.1.39: ribulose-bisphosphate carboxylase

This is an abbreviated version!
For detailed information about ribulose-bisphosphate carboxylase, go to the full flat file.

Reaction

2 3-phospho-D-glycerate + 2 H+ =

Synonyms

AF_1638, archaeal Rubisco, barley rubisco, Carboxydismutase, CbbL-1, CbbL-2, CbbL1 protein, CbbL2 protein, CbbM, CbbS-1, CbbS-2, D-ribulose 1,5-bisphosphate carboxylase/oxygenase, D-Ribulose 1,5-diphosphate carboxylase, D-Ribulose-1,5-bisphosphate carboxylase, D-ribulose-1,5-bisphosphate carboxylase/oxygenase, Diphosphoribulose carboxylase, form I RubisCO, Form II Rubisco, form III ribulose-1,5-bisphosphate carboxylase/oxygenase, Galdieria Rubisco, green-like type rubisco, LESS17, MbR, Pk-Rubisco, PSS15, PSSU1, Rbc, rbcL, RbcL2, rbcLS, rbcS, RbcS-T, rbcS1, red-type form I RuBisCO, ribulose 1, 5-bisphosphate carboxylase/oxygenase, ribulose 1,5 bisphosphate carboxylase/oxygenase, Ribulose 1,5-bisphosphate carboxylase, Ribulose 1,5-bisphosphate carboxylase-oxygenase, Ribulose 1,5-bisphosphate carboxylase/oxygenase, Ribulose 1,5-diphosphate carboxylase, Ribulose 1,5-diphosphate carboxylase/oxygenase, ribulose bisphosphate carboxylase, Ribulose bisphosphate carboxylase large chain, Ribulose bisphosphate carboxylase-oxygenase, ribulose bisphosphate carboxylase/oxygenase, ribulose bisphosphate carboxylase/oxygenase large subunit, Ribulose diphosphate carboxylase, Ribulose diphosphate carboxylase/oxygenase, ribulose-1, 5-bisphosphate carboxylase/oxygenase, ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase, ribulose-1,5-bisphosphate carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit, ribulose-bisphosphate carboxylase, ribulose-bisphosphate carboxylase/oxygenase, RLP, Rubisco, RubisCO 1, RuBisCO 2, RubisCO redlike form I, Rubisco small subunit, RuBisCO-like protein, Rubisco-LSU, RubiscoL, RuBP carboxylase, RuBP carboxylase/oxygenase, RuBPC, RuBPcase, RuBPCO, Tk-Rubisco, TK2290, type III ribulose 1,5-bisphosphate carboxylase/oxygenase, type III Rubisco, Water stress responsive proteins 1, 2 and 14

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.1 Carboxy-lyases

                4.1.1.39 ribulose-bisphosphate carboxylase

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Results	in table
33	Activating Compound
167638	AA Sequence
25	Application
1	CAS Registry Number
84	Cloned(Commentary)
70	Crystallization (Commentary)
28	Expression
81	General Information
7	General Stability
115	Inhibitors
56	kcat/KM [mM/s]
23	Ki Value [mM]
957	KM Value [mM]
132	Localization
107	Metals/Ions
208	Molecular Weight [Da]
395	Natural Substrates/ Products (Substrates)
735	Organism
2	Oxidation Stability
12	Pathway
961	PDB ID
36	pH Optimum
2	pH Range
1	pH Stability
4	pI Value
2	Posttranslational Modification
185	Protein Variants
133	Purification (Commentary)
167	Reaction
58	Reaction Type
659	Reference
170	Source Tissue
60	Specific Activity [micromol/min/mg]
16	Storage Stability
1088	Substrates and Products (Substrate)
118	Subunits
856	Synonyms
1	Systematic Name
36	Temperature Optimum [°C]
15	Temperature Range [°C]
20	Temperature Stability [°C]
394	Turnover Number [1/s]

Application

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Application on EC 4.1.1.39 - ribulose-bisphosphate carboxylase

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

agriculture

14 entries

analysis

3 entries

biofuel production

Synechocystis sp.

P54205

engineered cyanobacteria with enhanced growth show increased ethanol production and higher biofuel to biomass ratio. Speeding up the Calvin-Benson-Bassham cycle theoretically has positive effects on the subsequent growth and/or the end metabolite(s) production. Four Calvin-Benson-Bassham cycle enzymes, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase), transketolase (TK) and aldolase (FBA) are selected to be cooverexpressed with the ethanol synthesis enzymes pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) in the cyanobacterium Synechocystis PCC 6803. An inducible promoter, PnrsB, is used to drive pyruvate decarboxylaseC and alcohol dehydrogenase expression. When PnrsB is induced and cells are cultivated at 0.065 mM photons/m*s, the RuBisCO-, FBP/SBPase-, TK-, and FBA-expressing strains produce 55%, 67%, 37% and 69% more ethanol and 7.7%, 15.1%, 8.8% and 10.1% more total biomass (the sum of dry cell weight and ethanol), respectively, compared to the strain only expressing the ethanol biosynthesis pathway. The ethanol to total biomass ratio is also increased in Calvin-Benson-Bassham cycle enzymes overexpressing strains. Using the cells with enhanced carbon fixation, when the product synthesis pathway is not the main bottleneck, can significantly increase the generation of a product (exemplified with ethanol), which acts as a carbon sink

748559

biotechnology

3 entries

molecular biology

4 entries

agriculture

Synechococcus elongatus PCC 7942 = FACHB-805

-

target for increasing agricultural productivity

649333

agriculture

Spinacia oleracea

-

target for increasing agricultural productivity

649333

agriculture

Zea mays

-

target for increasing agricultural productivity

649333

agriculture

Nicotiana tabacum

-

target for increasing agricultural productivity

649333

agriculture

Solanum lycopersicum

-

target for increasing agricultural productivity

649333

agriculture

Helianthus annuus

-

target for increasing agricultural productivity

649333

agriculture

Oryza sativa

-

target for increasing agricultural productivity

649333

agriculture

Cylindrotheca sp.

-

target for increasing agricultural productivity

649333

agriculture

Chlorobaculum tepidum

-

target for increasing agricultural productivity

649333

agriculture

Flaveria bidentis

-

target for increasing agricultural productivity

649333

agriculture

Thermococcus kodakarensis

-

target for increasing agricultural productivity

649333

agriculture

Amphidinium carterae

-

target for increasing agricultural productivity

649333

agriculture

Hordeum vulgare

A0A0A1IXM9

replacment of native wheat Rubisco with Hordeum vulgare enzyme increases photosynthetic performance at 25°C and at 35°C. At 25°C Rubisco from Hordeum vulgare maximally increases the assimilation rate by 22%. Exchange of residue K14Q is the only difference relative to Triticum aestivum cv Cadenza

748325

agriculture

Aegilops cylindrica

A0A0A1IXH7

replacment of native wheat Rubisco with the enzyme increases photosynthetic performance at 25°C and at 35°C. At 25°C Rubisco from Aegilops cylindrica maximally increases the assimilation rate by 23%

748325

analysis

Arabidopsis thaliana

O03042

1 pg of plant mRNA, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, is used to determine the efficiency of RT-PCR in general, and as a external reference gene for normalization of gene expression

694208

analysis

Oryza sativa

-

a method is established to remove ribulose bisphosphate carboxylase/oxygenase from plant samples to obtain high quality and high resolution 2D gels in proteome analysis

693851

analysis

Nicotiana tabacum

-

a sensitive and robust mixed-mode high performance liquid chromatography-tandem mass spectrometry method is developed for the qualitative and quantitative determination of sugar phosphates

694678

biotechnology

Chlamydomonas reinhardtii

-

it is examined if recombinant protein accumulation can be enhanced by genetically fusing the recombinant reporter protein, luciferase, to the carboxy-terminal end of an abundant endogenous protein, the large subunit of ribulose bisphosphate carboxylase. A native protein-processing site from preferredoxin (preFd) is placed between the Rubisco LSU and luciferase coding regions in the fusion protein construct. Results demonstrate the utility of using fusion proteins to enhance recombinant protein accumulation in algal chloroplasts, and also show that engineered proteolytic processing sites can be used to liberate the exogenous protein from the endogenous fusion partner, allowing for the purification of the intended mature protein

702878

biotechnology

Chlamydomonas reinhardtii

-

Rubisco appears as suitable objective for biotechnological optimization of hydrogen production because of its relevance controlling the hydrogenase main competitor electron sink (the Calvin-Benson cycle), as well as starch accumulation and photorespiratory oxygen consumption

716997

biotechnology

Spinacia oleracea

-

RuBisCO protein readily forms a network with a very high gel strength, but upon deformation it has a brittle character (low critical strain, low fracture strain). RuBisCO exhibits high potential as a functional ingredient for the design of new textures at low protein concentration

747998

molecular biology

Symbiodinium sp.

Q41406

a continuous assay for Rubisco activity in crude cell extracts using the Mn2+ chemiluminescence of Rubisco oxygenase is described

706168

molecular biology

Triticum aestivum

-

a membrane inlet mass spectrometer method is developed that simultaneously determines the rate of Rubisco carboxylation (vc) and oxygenation (vo) and the CO2 and O2 concentrations

706166

molecular biology

Zea mays

-

a membrane inlet mass spectrometer method is developped that simultaneously determines the rate of Rubisco carboxylation (vc) and oxygenation (vo) and the CO2 and O2 concentrations

706166

molecular biology

Arachis hypogaea

-

proteome analysis of peanut leaf is conducted using two-dimensional gel electrophoresis in combination with sequence identification using MALDI/TOF. A master leaf polypeptide profile is generated based on the consistently expressed protein pattern. Proteins present in 205 spots are identified, including RuBisCO

705384