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Information on EC 6.3.4.B4 - ribulose bisphosphate carboxylase/oxygenase activase
for references in articles please use BRENDA:EC6.3.4.B4
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preliminary BRENDA-supplied EC number
EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.4 Other carbon-nitrogen ligases
6.3.4.B4 ribulose bisphosphate carboxylase/oxygenase activase
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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a [ribulose-bisphosphatcarboxylase]-L-lysine
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a [ribulose-bisphosphatcarboxylase]-L-lysine N6-carbamate
Synonyms
RCA, RCA1, rca2_alpha, RcaA1, RcaA2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
RCA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + a [ribulose-bisphosphatcarboxylase]-L-lysine + CO2 = ADP + phosphate + a [ribulose-bisphosphatcarboxylase]-L-lysine N6-carbamate
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-
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SYSTEMATIC NAME
IUBMB Comments
[ribulose-bisphosphate carboxylase]-N6-L-lysine:hydrogencarbonate ligase (ADP-forming)
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [ribulose-bisphosphatcarboxylase]-L-lysine + ?
ADP + phosphate + activated [ribulose-bisphosphatcarboxylase]
Substrates: -
Products: -
Products: -
?
ATP + [ribulose-bisphosphatcarboxylase]-L-lysine + CO2
ADP + phosphate + [ribulose-bisphosphatcarboxylase]-L-lysine N6-carbamate
ATP + [ribulose-bisphosphatcarboxylase]-L-lysine + CO2
ADP + phosphate + [ribulose-bisphosphatcarboxylase]-L-lysine N6-carbamate
Substrates: -
Products: -
Products: -
?
ATP + [ribulose-bisphosphatcarboxylase]-L-lysine + CO2
ADP + phosphate + [ribulose-bisphosphatcarboxylase]-L-lysine N6-carbamate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: activation of ribulose-bisphosphatcarboxylase is ATP-dependent. At high bicarbonate concentration, some spontaneous activation of rubisco occurseven in the absence of ATP. At 0.75 mM bicarbonate, activation of both endogenous and added rubisco is strictly ATP-dependent
Products: -
Products: -
-
additional information
?
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Substrates: enzyme additionally shows ATPase activity, reaction of EC 3.6.1.3
Products: -
Products: -
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphoenolpyruvate
3 millimolar, decreases the initial rate of activation, but the extent of activation is higher after 10 min
sulfosuccinimidyl-7-amino-4-methylcoumarin-3-acetate
-
treatment causes progressive inactivation of ATPase activity and concomitant loss of the ability to activate Rubisco. Second-order rate constant for inactivation is 239 per M and s, 1.9 mo1 of inhibitor is incorporated per mo1 of 42-kD Rubisco activase monomer. The primary site of modification is residue K247
-
sulfosuccinimidyl-acetate
-
treatment causes progressive inactivation of ATPase activity and concomitant loss of the ability to activate Rubisco. Second-order rate constant for inactivation is 21 per M and s
-
additional information
not inhibitiory: creatine phosphate or ATP, at 3 mM
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
after reduction by thioredoxin and dithiothreitol, the apparent dissociation constants (Kd) for ATPgammaS and Km of ATP hydrolysis of the large (46-kDa) isoform decreases to 60 and 40% of those of the oxidized form, respectively, and become more similar to those of the small (43-kDa) isoform
-
0.048
ATP
mutant C441S, K0.5 value, Hill slope 2.7, pH 8.0, 25°C
0.056
ATP
mutant K428R/C441S, K0.5 value, Hill slope 2.5, pH 8.0, 25°C
0.072
ATP
mutant K428R, K0.5 value, Hill slope 2.5, pH 8.0, 25°C
0.088
ATP
45 kDa isoform, S0.5 value, Hill coefficient 1.21, pH 8, 25°C
0.128
ATP
41 kDa isoform, S0.5 value, Hill coefficient 1.75, pH 8, 25°C
0.152
ATP
presence of 5 mM Mg2+ and 0.018 mM ADP, Hill coefficient 1.2, pH 8.0, 25°C
0.272
ATP
presence of 5 mM Mg2+ and 0.042 mM ADP, Hill coefficient 1.5, pH 8.0, 25°C
0.274
ATP
presence of 5 mM Mg2+ and 0.060 mM ADP, Hill coefficient 1.6, pH 8.0, 25°C
0.359
ATP
presence of 5 mM Mg2+ and 0.112 mM ADP, Hill coefficient 1.8, pH 8.0, 25°C
0.428
ATP
presence of 5 mM Mg2+ and 0.132 mM ADP, Hill coefficient 1.9, pH 8.0, 25°C
0.44
ATP
presence of 5 mM Mg2+ and 0.090 mM ADP, Hill coefficient 1.8, pH 8.0, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.72
ATP
presence of 5 mM Mg2+ and 0.132 mM ADP, Hill coefficient 1.9, pH 8.0, 25°C
0.88
ATP
presence of 5 mM Mg2+ and 0.042 mM ADP, Hill coefficient 1.5, pH 8.0, 25°C
0.93
ATP
presence of 5 mM Mg2+ and 0.090 mM ADP, Hill coefficient 1.8, pH 8.0, 25°C
1.15
ATP
presence of 5 mM Mg2+ and 0.060 mM ADP, Hill coefficient 1.6, pH 8.0, 25°C
1.41
ATP
presence of 5 mM Mg2+ and 0.018 mM ADP, Hill coefficient 1.2, pH 8.0, 25°C
1.45
ATP
presence of 5 mM Mg2+ and 0.112 mM ADP, Hill coefficient 1.8, pH 8.0, 25°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.29
0.72
additional information
under the optimum conditions of saturating CO2 (10 mM bicarbonate) and pH 8.0, the extent of spontaneous activation of the E form of substrate rubisco is more than 95% complete after 30 s. Measurement of maximum rubisco activase activity is performed at 25°C under the suboptimal conditions of pH 7.7 and 315 ppm CO2 and requires a high and constant ATP/ADP quotient
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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inhibition of Rubisco activation with concomitant formation of high-molecular weight aggregates at temperatures of 40°C or above. Inhibition is fully reversible below 40°C
40
inhibition of Rubisco activation with formation of high-molecular weight aggregates at temperatures of 40°C or above. Inhibition is fully reversible below 40°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform RcaA1, isoforms RcaA1 and RcaA2 are 99% identical, the 47 kDa isoform RcaA1 having an additional 33 amino acids and a 5 amino acid substitution at the carboxyl terminus
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
not detected in root or etiolated seedling tissues
brenda
specifically detected in leaf. During leaf development, the abundance of Osrca mRNAs increases from the 7th to the 3rd leaf
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
thylakoid membrane, enzyme shows a reversible association with the thylakoid membrane that is ATP and pH dependent. The amount of membrane-associated enzyme increases when the Rubisco activation state and the pH gradient across the thylakoid membrane decreases
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the C-extension of the large activase isoform plays an inhibitory role in ATP hydrolysis, regulated by redox changes. The C-extension of the oxidized large activase isoform can be cross-linked with regions containing residues that contribute to the nucleotide-binding pocket, with a higher efficiency in the presence of ADP or the absence of nucleotides than with ATP
metabolism
RCA hexameric ring asymmetry plays a critical functional role. A minimum of three different classes of sites exist. ATP hydrolysis is activated substantially by the cooperative binding of a second Mg2+ ion
metabolism
enzyme displays both ligase and ATPase activities. The two activities are not tightly coupled
physiological function
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at 25°C, activase transcript levels vary diurnally, peaking at the beginning of the photoperiod. Heat stress increases the accumulation of the 42-kDa activase isoform and induces a putative 41-kDa form. Heat stress does not affect the amounts of the 46- and 42-kDa activase isoforms. In contrast to activase, heat stress leads to a rapid and large reduction in the de novo synthesis of the large and small subunits of Rubisco
physiological function
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during the grain fillung period, a significant and gradual increase in Rubisco activity is seen. The highest Rubisco activity, photosynthetic rate and grain yield are found in the Z23 population, associated with increased leaf content of Rubisco activase protein
physiological function
rubisco activase and washed thylakoid membranes are sufficient to catalyze light stimulation of rubisco activation with a reconstituted system comprising ribulose bisphosphate carboxylase/oxygenase (rubisco), rubisco activase, washed thylakoid membranes, and ATP. Rubisco activase is required for this light stimulation. Light-dependent activation of rubisco in the reconstituted system is similar in whole-chain and PS I electron transport reactions, and saturated at approximately 100/miol photons per m2 and s
physiological function
rubisco activase activity is defined as the ability to promote activation of the inactive ribulose-1,5-bisphosphate-bound rubisco in an ATP-dependent reaction. The activation state of rubisco activase is independent of light intensity
physiological function
-
simultaneous increase in Rubisco and Rubisco activase contents leads to enhanced photosynthesis within the optimal temperature range. In transgenic rice plants cooverproducing both Rubisco and Rubisco activase, Rubisco content in increases by 23-44%, and Rubisco activase/Rubisco levels are similar or higher than those of wild-type plants, while the activation state of Rubisco is enhanced
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
in the presence of Mg-ATPgammS, the alpha (long) isoform of RCA forms predominantly closed hexamers with increased heat stability, whereas the beta (short) isoform forms a range of oligomers in solution with larger complexes forming at higher protein concentrations, analytical ultracentrifugation
additional information
?
-
x * 47000, calculated from sequence, x * 43000 and x * 47000, SDS-PAGE
?
x * 41000 and x * 45000, SDS-PAGE, 41 kDa isoform and 45 kDa isoform
additional information
-
Rubisco activase forms a wide range of structures in solution, ranging from monomers to much higher order species. The distribution of these species is highly dependent on protein concentration. Rubisco activase forms an open spiraling structure rather than a closed hexamericstructure. At protein concentrations of 1 microM, corresponding to the maximal activity of the enzyme, Rubisco activase has an oligomeric state of 2-4 subunits
additional information
-
heat stress increases the accumulation of the 42-kDa activase isoform and induces a putative 41-kDa form. Heat stress does not affect the amounts of the 46- and 42-kDa activase isoforms
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
growth of rice in the presence of 5 microM gibberellin A1 and addition of Ca 2+, Mg 2+, ATP into the reaction mixture stimulates phosphorylation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.9 A structure of the C-domain core of rubisco activase. The fold consists of a canonical four-helix bundle, from which a paddle-like extension protrudes that entails a nine-turn helix lined by an irregularly structured peptide strand. The residues Lys-313 and Val-316 involved in the species-specific recognition of Rubisco are located near the tip of the paddle. An ionic bond between Lys-313 and Glu-309 stabilizes the glycine-rich end of the helix
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C402Ins
insertion of a cysteine residue. In the absence of ADP, the mutant shows ATP hydrolysis and Rubisco activation activities comparable with those of wild-type. The mutant exhibits a similar redox-dependent sensitivity to ADP as the wild-type
D394A
mutation significantly reduces the sensitivity to ADP inhibition
D394A/E398A D401A
in the absence of ADP, the mutant shows 1.8fold higher ATP hydrolysis rate and 1.7fold higher Rubisco activation activity than the wild type. Mutant has 2.3fold higher ATPase and 3.6fold higher Rubisco activation activity than wild-type at an ADP/ATP ratio of 0.33
D401A
mutation significantly reduces the sensitivity to ADP inhibition
E390A
mutation significantly reduces the sensitivity to ADP inhibition
E390A/D401A
in the absence of ADP, the mutant shows 2.3fold higher ATP hydrolysis rate and 2.2fold higher Rubisco activation activity than the wild type. At an ADP/ATP ratio of 0.33, the mutant is much less sensitive to ADP inhibition with 4.6fold higher ATP hydrolysis and 6.6fold higher Rubisco activation activity than the wild type
R294A
-
mutation at the intersubunit interface. In the presence of Mg-ATPgammS, R294V protein forms a single species at all protein concentrations measured. Hexamers formed by R294V RCA are more stable complexes than wild-type hexamers
C256S
mutation in the 45-kD isoform reduces both Rubisco activase and ATPase activities
K107M
mutants displays reduced Rubisco activase and ATPase activities in both isoforms
Q109E
Rubisco activase activity increases in the 41-kD isoform, activity in the 45-kD isoform was similar to the wild-type enzyme. ATPase activity does not parallel the changes in Rubisco activase activity. Rather, a higher ratio of Rubisco activase to ATPase activity occurs in both isoforms
C441S
mutations in C-terminal extension, reduce inhibition by ADP
K428Q
mutation in C-terminal extension, reduces inhibition by ADP
K428R
mutation in C-terminal extension, reduces inhibition by ADP by increasing ATP substrate affinity and ATP-dependent catalytic velocity
K428R/C441S
mutations in C-terminal extension, reduce inhibition by ADP
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
41
15 min, presence of adenosine 5'-(gamma-thio)triphosphate, about 50% loss of activity, 41 kDa isoform
55
15 min, presence of adenosine 5'-(gamma-thio)triphosphate, about 50% loss of activity, 45 kDa isoform
additional information
40
formation of high-molecular weight aggregates at temperatures of 40°C or above
40
-
formation of high-molecular weight aggregates at temperatures of 40°C or above
additional information
presence of adenosine 5'-(gamma-thio)triphosphate, but not ADP, significantly enhances the thermostability of the 45 kDa form but is much less effective for the 41 kDa form
additional information
-
at 25°C, activase transcript levels vary diurnally, peaking at the beginning of the photoperiod. Heat stress increases the accumulation of the 42-kDa activase isoform and induces a putative 41-kDa form. Heat stress does not affect the amounts of the 46- and 42-kDa activase isoforms. In contrast to activase, heat stress leads to a rapid and large reduction in the de novo synthesis of the large and small subunits of Rubisco
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, by ammonium sulfate precipitation and Q-Sepharose fast protein liquid chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
co-overexpression of the Arabidopsis thaliana gene AVP1 and the Larrea tridentata Rubisco activase gene RCA in Arabidopsis thaliana significantly increases drought, salinity and heat tolerance, resulting in higher biomass and seed yield than wild-type plants. AVP1/RCA cooverexpressing plants are as more drought- and salt-tolerant as AVP1-overexpressing plants, and as more heat-tolerant as RCA-overexpressing plants. They produce higher seed yields than AVP1-overexpressing, RCA-overexpressing, and wild-type plants under combined drought and heat conditions
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Law, R.D.; Crafts-Brandner, S.J.
High temperature stress increases the expression of wheat leaf ribulose-1,5-bisphosphate carboxylase/oxygenase activase protein
Arch. Biochem. Biophys.
386
261-267
2001
Triticum aestivum
brenda
Keown, J.R; Pearce, F.G.
Characterization of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase activase isoforms reveals hexameric assemblies with increased thermal stability
Biochem. J.
464
413-423
2014
Nicotiana tabacum, Spinacia oleracea (P10871)
brenda
Komatsu, S.; Masuda, T.; Hirano, H.
Rice gibberellin-binding phosphoprotein structurally related to ribulose-1,5-bisphosphate carboxylase/oxygenase activase
FEBS Lett.
384
167-171
1996
Oryza sativa Japonica Group
brenda
Zhang, Z.; Komatsu, S.
Molecular cloning and characterization of cDNAs encoding two isoforms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in rice (Oryza sativa L.)
J. Biochem.
128
383-389
2000
Oryza sativa Japonica Group (P93431)
brenda
Wang, D.; Portis, A.R.
Increased sensitivity of oxidized large isoform of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase to ADP inhibition is due to an interaction between its carboxyl extension and nucleotide-binding pocket
J. Biol. Chem.
281
25241-25249
2006
Arabidopsis thaliana (P10896)
brenda
Henderson, J.N.; Kuriata, A.M.; Fromme, R.; Salvucci, M.E.; Wachter, R.M.
Atomic resolution x-ray structure of the substrate recognition domain of higher plant ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase
J. Biol. Chem.
286
35683-35688
2011
Larrea tridentata (Q7X9A0)
brenda
Keown, J.R.; Griffin, M.D.W.; Mertens, H.D.T.; Pearce, F.G.
Small oligomers of ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase are required for biological activity
J. Biol. Chem.
288
20607-20615
2013
Nicotiana tabacum
brenda
Hazra, S.; Henderson, J.N.; Liles, K.; Hilton, M.T.; Wachter, R.M.
Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase product inhibition, cooperativity, and magnesium activation
J. Biol. Chem.
290
24222-24236
2015
Nicotiana tabacum (Q40565)
brenda
Scafaro, A.P.; De Vleesschauwer, D.; Bautsoens, N.; Hannah, M.A.; den Boer, B.; Galle, A.; Van Rie, J.
A single point mutation in the C-terminal extension of wheat Rubisco activase dramatically reduces ADP inhibition via enhanced ATP binding affinity
J. Biol. Chem.
294
17931-17940
2019
Triticum aestivum (A0A078BQY4)
brenda
Morales, A.; Ortega-Delgado, M.L.; Molina-Galan, J.; Sanchez de Jimenez, E.
Importance of Rubisco activase in maize productivity based on mass selection procedure
J. Exp. Bot.
335
823-829
1999
Zea mays
-
brenda
Chen, J.; Wang, P.; Mi, H.-L.; Chen, G.-Y.; Xu, D.-Q.
Reversible association of ribulose-1, 5-bisphosphate carboxylase/oxygenase activase with the thylakoid membrane depends upon the ATP level and pH in rice without heat stress
J. Exp. Bot.
61
2939-50
2010
Oryza sativa Japonica Group (P93431)
brenda
Campbell, W.J.; Ogren, W.L.
Light activation of Rubisco by Rubisco activase and thylakoid membranes
Plant Cell Physiol.
33
751-756
1992
Spinacia oleracea (P10871)
-
brenda
Campbell, W.J.; Ogren, W.L.
Rubisco activase activity in spinach leaf extracts
Plant Cell Physiol.
36
215-220
1995
Spinacia oleracea (P10871)
-
brenda
Salvucci, M.E.
Covalent modification of a highly reactive and essential lysine residue of ribulose-1,5-bisphosphate carboxylase/oxygenase activase
Plant Physiol.
103
501-508
1993
Nicotiana tabacum
brenda
Crafts-Brandner, S.J.; Van De Loo, F.J.; Salvucci, M.E.
The two forms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase differ in sensitivity to elevated temperature
Plant Physiol.
114
439-444
1997
Spinacia oleracea (P10871)
brenda
Feller, U.; Crafts-Brandner, S.J.; Salvucci, M.E.
Moderately high temperatures inhibit ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco
Plant Physiol.
116
539-546
1998
Gossypium hirsutum (Q9AXG1), Triticum aestivum
brenda
Suganami, M.; Suzuki, Y.; Tazoe, Y.; Yamori, W.; Makino, A.
Co-overproducing Rubisco and Rubisco activase enhances photosynthesis in the optimal temperature range in rice
Plant Physiol.
185
108-119
2021
Oryza sativa
brenda
Lilley, R.M.; Portis, A.R.
Activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) by rubisco activase effects of some sugar phosphates
Plant Physiol.
94
245-250
1990
Spinacia oleracea (P10871)
brenda
Shen, J.B.; Ogren, W.L.
Alteration of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase activase activities by site-directed mutagenesis
Plant Physiol.
99
1201-1207
1992
Spinacia oleracea (P10871)
brenda
Wijewardene, I.; Mishra, N.; Sun, L.; Smith, J.; Zhu, X.; Payton, P.; Shen, G.; Zhang, H.
Improving drought-, salinity-, and heat-tolerance in transgenic plants by co-overexpressing Arabidopsis vacuolar pyrophosphatase gene AVP1 and Larrea Rubisco activase gene RCA
Plant Sci.
296
110499
2020
Larrea tridentata (Q7X9A0)
brenda
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