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Information on EC 4.1.1.39 - ribulose-bisphosphate carboxylase and Organism(s) Rhodospirillum rubrum and UniProt Accession P04718
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4.1.1.39 ribulose-bisphosphate carboxylaseIUBMB Comments
Will utilize O2 instead of CO2, forming 3-phospho-D-glycerate and 2-phosphoglycolate.
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Word Map
- 4.1.1.39
- co2
- chloroplast
- chlorophyll
-
stomatal
- plastid
- mesophyll
- activase
- photosystems
- spinach
- seedling
- dioxide
- thylakoids
- phosphoenolpyruvate
- wheat
-
photorespiration
-
atmospheric
- maize
-
acclimation
- chlamydomonas
- cyanobacteria
- drought
- reinhardtii
-
autotroph
-
photochemical
- anhydrase
-
photorespiratory
-
calvin
-
climate
-
light-harvesting
-
transpiration
-
nuclear-encoded
- rubrum
- aestivum
- triticum
- rhodospirillum
- 3-phosphoglycerate
-
canopy
- synechococcus
- phosphoribulokinase
-
photoautotrophic
-
photochemistry
- analysis
-
crassulacean
- molecular biology
- lhcii
- biotechnology
-
photoinhibition
-
non-photochemical
-
carbamylation
- carboxylases
-
nadp-malic
- dikinase
-
oxygen-evolving
- biofuel production
- agriculture
The taxonomic range for the selected organisms is: Rhodospirillum rubrum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
rubisco, ribulose-1,5-bisphosphate carboxylase/oxygenase, ribulose-1,5-bisphosphate carboxylase, rubpcase, ribulose bisphosphate carboxylase, ribulose 1,5-bisphosphate carboxylase/oxygenase, ribulose 1,5-bisphosphate carboxylase, ribulose bisphosphate carboxylase/oxygenase, rubp carboxylase, rubisco small subunit, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Carboxydismutase
-
-
-
-
D-Ribulose 1,5-diphosphate carboxylase
-
-
-
-
D-Ribulose-1,5-bisphosphate carboxylase
-
-
-
-
Diphosphoribulose carboxylase
-
-
-
-
LESS17
-
-
-
-
PSS15
-
-
-
-
PSSU1
-
-
-
-
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-oxygenase
-
-
-
-
Ribulose diphosphate carboxylase
-
-
-
-
Ribulose diphosphate carboxylase/oxygenase
-
-
-
-
Rubisco
RuBP carboxylase
-
-
-
-
Water stress responsive proteins 1, 2 and 14
-
-
-
-
Ribulose 1,5-bisphosphate carboxylase/oxygenase
-
-
-
-
Ribulose 1,5-bisphosphate carboxylase/oxygenase
-
-
Rubisco
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O
D-ribulose 1,5-bisphosphate + CO2 = 2 3-phospho-D-glycerate, carboxylase reaction
-
2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O
D-Ribulose 1,5-bisphosphate + O2 = D-3-phosphoglycerate + 2-phosphoglycolate, oxygenase reaction
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
oxygenation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
3-phospho-D-glycerate carboxy-lyase (dimerizing; D-ribulose-1,5-bisphosphate-forming)
Will utilize O2 instead of CO2, forming 3-phospho-D-glycerate and 2-phosphoglycolate.
CAS REGISTRY NUMBER
COMMENTARY
9027-23-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-phospho-D-glycerate + H+
D-ribulose 1,5-bisphosphate + CO2 + H2O
-
-
-
r
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
-
-
?
D-ribulose 1,5-bisphosphate + O2
2-phosphoglycolate + 3-phospho-D-glycerate
-
-
-
?
D-ribulose 1,5-bisphosphate + O2
3-phospho-D-glycerate + 2-phosphoglycolate
-
-
-
?
5-(methylsulfanyl)-2,3-dioxopentyl phosphate
(1Z)-2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-en-1-yl phosphate
-
the form II RubisCO enzyme from Rhodospirillum rubrum is also able to function as an enolase in vivo as part of an methionine salvage pathway, but only under anaerobic conditions
-
-
?
D-Ribulose 1,5-bisphosphate + CO2
?
-
-
-
-
?
D-Ribulose 1,5-bisphosphate + CO2
D-3-Phosphoglycerate
-
-
-
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
2 3-phospho-D-glycerate + 2 H+
-
-
-
-
r
D-Ribulose 1,5-bisphosphate + O2
D-3-Phosphoglycerate + 2-phosphoglycolate
-
-
-
-
?
D-ribulose 1,5-bisphosphate + O2
pentodiulose-1,5-bisphosphate + H2O2
-
enzyme from Rhodospirillum rubrum produces more H2O2 than the enzyme from Spinacia oleracea
-
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
-
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
-
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
-
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
-
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
-
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
-
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
-
-
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
Calvin-Benson-Bassham reductive pentose phosphate pathway, first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation, as the entry point of CO2 into the biosphere, enzyme is central to life on earth
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation, CO2 fixing enzyme that enables most forms of photo-and chemoautotrophic life
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
key enzyme responsible for photosynthetic carbon assimilation and photorespiratory carbon oxidation
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
rate-limiting reaction of overall photosynthetic CO2 assimilation and photorespiratory carbon oxidation
-
ir
D-ribulose 1,5-bisphosphate + O2
3-phospho-D-glycerate + 2-phosphoglycolate
-
-
-
?
D-ribulose 1,5-bisphosphate + O2
3-phospho-D-glycerate + 2-phosphoglycolate
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-phospho-D-glycerate + H+
D-ribulose 1,5-bisphosphate + CO2 + H2O
-
-
-
r
D-ribulose 1,5-bisphosphate + O2
2-phosphoglycolate + 3-phospho-D-glycerate
-
-
-
?
D-Ribulose 1,5-bisphosphate + CO2
?
-
-
-
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
Calvin-Benson-Bassham reductive pentose phosphate pathway, first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation, as the entry point of CO2 into the biosphere, enzyme is central to life on earth
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation, CO2 fixing enzyme that enables most forms of photo-and chemoautotrophic life
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
key enzyme responsible for photosynthetic carbon assimilation and photorespiratory carbon oxidation
-
?
D-ribulose 1,5-bisphosphate + CO2 + H2O
3-phospho-D-glycerate
-
rate-limiting reaction of overall photosynthetic CO2 assimilation and photorespiratory carbon oxidation
-
ir
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Co2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glycero-2,3-pentodiulose-1,5-bisphosphate
-
potent inhibitor of activity with D-ribulose 1,5-bisphosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.128
CO2
-
wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
0.256
CO2
-
mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
0.03
D-ribulose 1,5-bisphosphate
-
wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
0.0567
D-ribulose 1,5-bisphosphate
-
mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
CO2
-
mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
5
CO2
-
wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
3
D-ribulose 1,5-bisphosphate
-
mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
5
D-ribulose 1,5-bisphosphate
-
wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12
CO2
-
mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
39
CO2
-
wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
54
D-ribulose 1,5-bisphosphate
-
mutant enzyme K122R, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
160
D-ribulose 1,5-bisphosphate
-
wild type enzyme, in CO2- and O2-free 200 mM Bicine-NaOH buffer (pH 8.0) containing 20 mM MgCl2, at 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.245
D-fructose-1,6-bisphosphate
mutant enzyme D117H, at 25°C, pH 8
0.32
D-fructose-1,6-bisphosphate
mutant enzyme H44N, at 25°C, pH 8
0.347
D-fructose-1,6-bisphosphate
mutant enzyme D117V, at 25°C, pH 8
0.348
D-fructose-1,6-bisphosphate
mutant enzyme H44Q, at 25°C, pH 8
0.465
D-fructose-1,6-bisphosphate
wild type enzyme, at 25°C, pH 8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the catalytic incorporation of CO2 into D-ribulose 1,5-bisphosphate by Rubisco is the first step in the production of carbohydrates by plants, which are used to build biomass and produce energy during growth and development
malfunction
-
the form II RubisCO disruption strain is able to grow using 5-methylthioadenosine as the sole sulfur source
metabolism
-
RubisCO is the key enzyme of the Calvin-Benson-Bassham reductive pentose phosphate pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D263A
kcat and Km (substrate: CO2) (substrate: D-ribulose 1,5-bisphosphate) are reduced compared to wildtype
D263E
kcat and Km (substrate: CO2) (substrate: D-ribulose 1,5-bisphosphate) are reduced compared to wildtype, mutant D263E has a significantly higher Km value for (substrate: CO2) compared to mutant D263N (although both mutants have approximately the same kcat value)
D263N
kcat and Km (substrate: CO2) (substrate: D-ribulose 1,5-bisphosphate) are reduced compared to wildtype, mutant D263N has a significantly lower Km value for (substrate: CO2) compared to mutant D263N (although both mutants have approximately the same kcat value)
D263Q
D263Q shows the lowest value for kcat and Km (substrate: CO2) (substrate: D-ribulose 1,5-bisphosphate)
D263S
kcat and Km (substrate: CO2) (substrate: D-ribulose 1,5-bisphosphate) are reduced compared to wildtype
C58S
-
site-directed mutagenesis, elimination of the chemically active site without any loss of activity
K122E
-
the mutant is almost inactive (0.8% activity compared to the wild type enzyme)
K122M
-
the mutant is almost inactive (0.2% activity compared to the wild type enzyme)
K122R
-
the mutant with 69% activity compared to the wild type enzyme has a 40% decrease in kcat for carboxylase activity, a 2fold increase in Km for CO2, and a 1.9fold increase in Km for D-ribulose 1,5-bisphosphate
K166C
-
site-directed mutagenesis, able to process RuBP, but the major product is DiMP derived from beta-elimination of phosphate from the enediol
K166C/C58S
-
site-directed mutagenesis, virtually inactive double mutant
K166G
-
site-directed mutagenesis, able to process RuBP, but the major product is DiMP derived from beta-elimination of phosphate from the enediol
K166S
-
site-directed mutagenesis, able to process RuBP, but the major product is DiMP derived from beta-elimination of phosphate from the enediol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant rbc genes transferred into pFL260 for expression in Escherichia coli MV1190
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Terzaghi, B.E.; Laing, W.A.; Christeller, J.T.; Petersen, G.B.; Hill, D.F.
Ribulose 1,5-bisphosphate carboxylase. Effect on the catalytic properties of changing methionine-330 to leucine in the Rhodospirillum rubrum enzyme
Biochem. J.
235
839-846
1986
Rhodospirillum rubrum
Jordan, D.B.; Ogren, W.L.
Species variation in kinetic properties of ribulose 1,5-bisphosphate carboxylase/oxygenase
Arch. Biochem. Biophys.
227
425-433
1983
Amaranthus hybridus, Aphanizomenon flos-aquae, Aphanocapsa alpicola, Echinochloa crus-galli, Glycine max, Helianthus maximus, Medicago sativa, Solanum lycopersicum, Nicotiana tabacum, Panicum milioides, Petroselinum crispum, Plectonema borganum, Polypodium aureum, Portulaca oleracea, Rhodospirillum rubrum, Setaria italica, Sorghum bicolor, Spinacia oleracea, Zea mays
Schloss, J.V.; Phares, E.F.; Long, M.V.; Norton, I.L.; Stringer, C.D.; Hartman, F.C.
Ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum
Methods Enzymol.
90
522-528
1982
Rhodospirillum rubrum
Schloss, J.V.; Phares, E.F.; Long, M.V.; Norton, I.L.; Stringer, C.D.; Hartman, F.C.
Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum
J. Bacteriol.
137
490-501
1979
Rhodospirillum rubrum
Anderson, L.E.
Ribulose-1,5-diphosphate carboxylase from Rhodospirillum rubrum
Methods Enzymol.
42C
457-461
1975
Rhodospirillum rubrum
McFadden, B.A.; Tabita, F.R.; Kuehn, G.D.
Ribulose-diphosphate carboxylase from the hydrogen bacteria and Rhodospirillum rubrum
Methods Enzymol.
42C
461-472
1975
Cupriavidus necator, Acidovorax facilis, Rhodospirillum rubrum
Smith, H.B.; Larimer, F.W.; Hartman, F.C.
An engineered change in substrate specificity of ribulosebisphosphate carboxylase/oxygenase
J. Biol. Chem.
265
1243-1245
1990
Rhodospirillum rubrum
Spreitzer, R.J.; Salvucci, M.E.
Rubisco: Structure, regulatory interactions, and possibilities for a better enzyme
Annu. Rev. Plant Biol.
53
449-475
2002
Cupriavidus necator, Anabaena sp., Trichormus variabilis, Synechococcus elongatus PCC 7942 = FACHB-805, Arabidopsis thaliana, Chlamydomonas reinhardtii, Chlorobaculum tepidum, Cylindrotheca sp., Flaveria bidentis, Galdieria partita, Helianthus annuus, Solanum lycopersicum, Nicotiana tabacum, Oryza sativa, Thermococcus kodakarensis, Rhodospirillum rubrum, Spinacia oleracea, Synechococcus sp., Zea mays, Amphidinium carterae, Anabaena sp. CA
John Andrews, T.; Whitney, S.M.
Manipulating ribulose bisphosphate carboxylase/oxygenase in the chloroplasts of higher plants
Arch. Biochem. Biophys.
414
159-169
2003
Synechocystis sp., Arabidopsis thaliana, Flaveria bidentis, Galdieria sulphuraria, Nicotiana tabacum, Oryza sativa, Phaeodactylum tricornutum, Rhodospirillum rubrum, Griffithsia monilis
Harpel, M.R.; Larimer, F.W.; Hartman, F.C.
Multifaceted roles of Lys166 of ribulose-bisphosphate carboxylase/oxygenase as discerned by product analysis and chemical rescue of site-directed mutants
Biochemistry
41
1390-1397
2002
Rhodospirillum rubrum
Parry, M.A.; Andralojc, P.J.; Mitchell, R.A.; Madgwick, P.J.; Keys, A.J.
Manipulation of Rubisco: the amount, activity, function and regulation
J. Exp. Bot.
54
1321-1333
2003
Allochromatium vinosum, Arabidopsis thaliana, Avena sativa, Chlamydomonas reinhardtii, Cylindrotheca sp., Flaveria bidentis, Galdieria partita, Galdieria sulphuraria, Glycine max, Helianthus annuus, Hordeum vulgare, Solanum lycopersicum, Nicotiana tabacum, Olisthodiscus luteus, Oryza sativa, Petunia sp., Phaeodactylum tricornutum, Pisum sativum, Rhodobacter capsulatus, Cereibacter sphaeroides, Rhodospirillum rubrum, Spinacia oleracea, Triticum aestivum, Zea mays, Cylindrotheca sp. N1
Tabita, F.R.
Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A different perspective
Photosynth. Res.
60
1-28
1999
Acidithiobacillus ferrooxidans, Cupriavidus necator, Allochromatium vinosum, Anabaena sp., Archaeoglobus fulgidus, Bacillus subtilis, Bradyrhizobium japonicum, Chlorobium limicola, Chlorobaculum tepidum, Cyanidium caldarium, Cylindrotheca fusiformis, Cylindrotheca sp., Galdieria partita, Haloferax sp., Hydrogenovibrio marinus, Methanocaldococcus jannaschii, Nicotiana tabacum, Olisthodiscus luteus, Porphyridium purpureum, Pyrococcus sp., Pyrococcus horikoshii, Thermococcus kodakarensis, Rhodobacter capsulatus, Cereibacter sphaeroides, Rhodospirillum rubrum, Synechococcus sp., Thiobacillus denitrificans, Thiomonas intermedia, Halothiobacillus neapolitanus, Xanthobacter flavus, Trematocarpus dichotomus, Amphidinium carterae, Symbiodinium sp., Hydrogenovibrio marinus L2, Synechococcus sp. 6301, Cylindrotheca sp. N1
-
Schlitter, J.; Wildner, G.F.
The kinetics of conformation change as determinant of Rubisco's specificity
Photosynth. Res.
65
7-13
2000
Galdieria partita, Rhodospirillum rubrum, Spinacia oleracea, Synechococcus sp.
Kim, K.; Portis, A.R., Jr.
Oxygen-dependent H2O2 production by Rubisco
FEBS Lett.
571
124-128
2004
Chlamydomonas reinhardtii, Rhodospirillum rubrum, Spinacia oleracea
Mueller-Cajar, O.; Morell, M.; Whitney, S.M.
Directed evolution of Rubisco in Escherichia coli reveals a specificity-determining hydrogen bond in the form II enzyme
Biochemistry
46
14067-14074
2007
Rhodospirillum rubrum (P04718), Rhodospirillum rubrum
Tcherkez, G.G.; Farquhar, G.D.; Andrews, T.J.
Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized
Proc. Natl. Acad. Sci. USA
103
7246-7251
2006
Allochromatium vinosum, Amaranthus hybridus, Trichormus variabilis, Chlamydomonas reinhardtii, Euglena gracilis, Galdieria sulphuraria, Nicotiana tabacum, Oryza sativa, Phaeodactylum tricornutum, Rhodospirillum rubrum, Sorghum bicolor, Spinacia oleracea, Synechococcus sp., Triticum aestivum, Zea mays, Griffithsia monilis, Atriplex glabriuscula, Synechococcus sp. 6301, Synechococcus sp. 7002
Andersson, I.; Backlund, A.
Structure and function of Rubisco
Plant Physiol. Biochem.
46
275-291
2008
Cupriavidus necator, Chlorobaculum tepidum, Galdieria partita, Nicotiana tabacum, Thermococcus kodakarensis, Rhodopseudomonas palustris, Synechococcus sp., Halothiobacillus neapolitanus, Geobacillus kaustophilus, Spinacia oleracea (O20253), Pyrococcus horikoshii (O58677), Rhodospirillum rubrum (P04718), Chlamydomonas reinhardtii (P08475), Oryza sativa (Q0INY7)
Liggins, J.R.; Gready, J.E.
Putative functional role for the invariant aspartate 263 residue of Rhodospirillum rubrum Rubisco
Biochemistry
48
2226-2236
2009
Rhodospirillum rubrum (P04718), Rhodospirillum rubrum
Witzel, F.; Goetze, J.; Ebenhoeh, O.
Slow deactivation of ribulose 1,5-bisphosphate carboxylase/oxygenase elucidated by mathematical models
FEBS J.
277
931-950
2010
Galdieria sulphuraria, Nicotiana tabacum, Phaeodactylum tricornutum, Rhodospirillum rubrum, Synechococcus sp., Griffithsia monilis
Nakano, T.; Ashida, H.; Mizohata, E.; Matsumura, H.; Yokota, A.
An evolutionally conserved Lys122 is essential for function in Rhodospirillum rubrum bona fide RuBisCO and Bacillus subtilis RuBisCO-like protein
Biochem. Biophys. Res. Commun.
392
212-216
2010
Rhodospirillum rubrum
Singh, J.; Tabita, F.
Roles of RubisCO and the RubisCO-like protein in 5-methylthioadenosine metabolism in the nonsulfur purple bacterium Rhodospirillum rubrum
J. Bacteriol.
192
1324-1331
2010
Rhodospirillum rubrum, Rhodospirillum rubrum Str-2
Whitney, S.; Houtz, R.; Alonso, H.
Advancing our understanding and capacity to engineer natures CO2-sequestering enzyme, Rubisco
Plant Physiol.
155
27-35
2011
Pyrococcus horikoshii (O58677), Thermococcus kodakarensis (O93627), Spinacia oleracea (P00870), Spinacia oleracea (P00875), Rhodospirillum rubrum (P04718)
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