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Information on EC 2.7.1.19 - phosphoribulokinase
for references in articles please use BRENDA:EC2.7.1.19
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.19 phosphoribulokinase
The enzyme appears in viruses and cellular organisms
- 2.7.1.19
- chloroplast
- co2
-
calvin
- rubisco
- ribulose-1,5-bisphosphate
- carboxylase
- spinach
- chlamydomonas
- reinhardtii
- fructose-1,6-bisphosphatase
- sphaeroides
-
calvin-benson
- rubp
- ribose-5-phosphate
-
calvin-benson-bassham
- fbpase
- sedoheptulose-1,7-bisphosphatase
-
1.2.1.13
-
nadp-malate
-
4.1.1.39
-
1,6-bisphosphatase
-
co2-fixing
- 1,5-diphosphate
- arecaceae
-
thioredoxin-mediated
- sedoheptulose
-
nadp-glyceraldehyde-3-phosphate
-
photoheterotrophic
showSynonyms
phosphoribulokinase, ribulose-5-phosphate kinase, ribulose 5-phosphate kinase, crprk, atprk, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-phosphoribulose kinase
-
-
-
-
glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase
kinase, phosphoribulo- (phosphorylating)
-
-
-
-
Mext_0980
phosphopentokinase
-
-
-
-
phosphoribulokinase
PKK
-
-
-
-
Prk
PRuK
-
-
-
-
ribulose 5-phosphate kinase
-
-
-
-
ribulose phosphate kinase
-
-
-
-
ribulose-5-phosphate kinase
-
-
-
-
SePRK
synpcc7942_0977
glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase
-
glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase form a supramolecular complex with the regulatory peptide CP12, both enzyme activities strongly dependent on complex formation
glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase
-
glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase form a supramolecular complex with the regulatory peptide CP12, both enzyme activities strongly dependent on complex formation
Prk
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate
mechanism
-
ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate
mechanism
-
ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
Calvin-Benson-Bassham cycle, Rubisco shunt
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-ribulose-5-phosphate 1-phosphotransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9030-60-8
-
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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
D-fructose 6-phosphate + ATP
?
-
Substrates: 3.6% of ribulose 5-phosphate activity
Products: -
Products: -
?
D-ribose 5-phosphate + ATP
D-ribose 1,5-diphosphate + ADP
-
Substrates: -
Products: PRK activity of multienzyme complexes is higher with D-ribose-5-phosphate and ATP than in the presence of D-ribulose 5-phosphate
Products: PRK activity of multienzyme complexes is higher with D-ribose-5-phosphate and ATP than in the presence of D-ribulose 5-phosphate
?
D-ribulose 5-phosphate + GTP
D-ribulose 1,5-diphosphate + GDP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + trinitrophenyl-ATP
D-ribulose 1,5-diphosphate + trinitrophenyl-ADP
D-ribulose 5-phosphate + UTP
D-ribulose 1,5-diphosphate + UDP
-
Substrates: -
Products: -
Products: -
?
sedoheptulose 7-phosphate + ATP
?
-
Substrates: 2.5% of ribulose 5-phosphate activity
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: part of the Calvin cycle (reductive pentose phosphate pathway), involved in CO2 fixation in photosynthetic organisms
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: the ATP binding site is disrupted in the oxidized enzyme (PRK), whereas the D-ribulose 5-phosphate binding site is occupied by oxidized chloroplast protein CP12 in the glyceraldehyde-3-phosphate dehydrogenase/CP12/PRK complex
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: part of the Calvin cycle (reductive pentose phosphate pathway), involved in CO2 fixation in photosynthetic organisms
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
A9W1C9
Substrates: the Calvin cycle enzyme phosphoribulokinase is essential for growth on methanol. Ribulose-1,5-bisphosphate is crucial for the regulation of one-carbon assimilation
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
A9W1C9
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
A9W1C9
Substrates: the Calvin cycle enzyme phosphoribulokinase is essential for growth on methanol. Ribulose-1,5-bisphosphate is crucial for the regulation of one-carbon assimilation
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
A9W1C9
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: part of the Calvin cycle (reductive pentose phosphate pathway), involved in CO2 fixation in photosynthetic organisms
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: the ATP binding site is disrupted in the oxidized enzyme (PRK), whereas the D-ribulose 5-phosphate binding site is occupied by oxidized chloroplast protein CP12 in the glyceraldehyde-3-phosphate dehydrogenase/CP12/PRK complex
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: the ATP binding site is disrupted in the oxidized enzyme (PRK), whereas the D-ribulose 5-phosphate binding site is occupied by oxidized chloroplast protein CP12 in the glyceraldehyde-3-phosphate dehydrogenase/CP12/PRK complex
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: part of the Calvin cycle (reductive pentose phosphate pathway), involved in CO2 fixation in photosynthetic organisms
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by CTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by UTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by GTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: interaction with glyceraldehydes-3-phosphate may play a role in regulation of calvin cycle
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: interaction with glyceraldehydes-3-phosphate may play a role in regulation of calvin cycle
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by UTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by GTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
Diacronema lutheri 926-1
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: key enzyme in reductive pentose-phosphate cycle
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by CTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by UTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by GTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by TTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by CTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by UTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by GTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: ATP can be substituted by TTP with reduced activity
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + trinitrophenyl-ATP
D-ribulose 1,5-diphosphate + trinitrophenyl-ADP
-
Substrates: -
Products: -
Products: -
?
D-ribulose 5-phosphate + trinitrophenyl-ATP
D-ribulose 1,5-diphosphate + trinitrophenyl-ADP
-
Substrates: spectroscopically active ATP-analog
Products: -
Products: -
?
additional information
?
-
-
Substrates: association between binding protein CP12 and phosphoribulokinase (EC 2.7.1.19), glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.13) and aldolase. The dissociation constant between CP12 and fructose 1,6-bisphosphate (EC 4.1.2.13) aldolase is 0.00048 mM and thus corroborates an interaction between CP12 and aldolase. The dissociation constant between aldolase and the phosphoribulokinase/lyceraldehyde 3-phosphate dehydrogenase/CP12 complex is 55 mM
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with fructose 6-phosphate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: association between binding protein CP12 and phosphoribulokinase (EC 2.7.1.19), glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.13) and aldolase. The dissociation constant between CP12 and fructose 1,6-bisphosphate (EC 4.1.2.13) aldolase is 0.00048 mM and thus corroborates an interaction between CP12 and aldolase. The dissociation constant between aldolase and the phosphoribulokinase/lyceraldehyde 3-phosphate dehydrogenase/CP12 complex is 55 mM
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: part of the Calvin cycle (reductive pentose phosphate pathway), involved in CO2 fixation in photosynthetic organisms
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: part of the Calvin cycle (reductive pentose phosphate pathway), involved in CO2 fixation in photosynthetic organisms
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ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
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ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
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ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
A9W1C9
Substrates: the Calvin cycle enzyme phosphoribulokinase is essential for growth on methanol. Ribulose-1,5-bisphosphate is crucial for the regulation of one-carbon assimilation
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ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
A9W1C9
Substrates: the Calvin cycle enzyme phosphoribulokinase is essential for growth on methanol. Ribulose-1,5-bisphosphate is crucial for the regulation of one-carbon assimilation
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ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
-
Substrates: -
Products: -
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?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: part of the Calvin cycle (reductive pentose phosphate pathway), involved in CO2 fixation in photosynthetic organisms
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: -
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
Products: -
Products: -
?
ATP + D-ribulose 5-phosphate
ADP + D-ribulose 1,5-bisphosphate
Substrates: part of the Calvin cycle (reductive pentose phosphate pathway), involved in CO2 fixation in photosynthetic organisms
Products: -
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?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: interaction with glyceraldehydes-3-phosphate may play a role in regulation of calvin cycle
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: interaction with glyceraldehydes-3-phosphate may play a role in regulation of calvin cycle
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?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: key enzyme in reductive pentose-phosphate cycle
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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?
D-ribulose 5-phosphate + ATP
D-ribulose 1,5-diphosphate + ADP
-
Substrates: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
DTNB, Ellmans reagent, almost complete inhibition at 0.0045 mM
6-phosphogluconate
-
competitive inhibitor, 78% residual activity at 1 mM
cystine
-
oxidized form, inhibition almost completely reversible by addition of reduced dithiothreitol
regulatory protein CP12
-
forming under oxidizing conditions a supramolecular complex (2 phosphoribulokinase dimers + 2 glyceraldehyde-3-phosphate dehydrogenase tetramers + 4 CP12 monomers)
-
6-phospho-D-gluconate
-
competitive with respect to D-ribulose 5-phosphate
dithiothreitol
-
light- and dark-adapted extract prepared and assayed without reducing agent, is not significantly affected by incubation with reduced dithiothreitol, however, subsequent incubation with oxidized dithiothreitol results in a significant reduction of enzyme activity under both light and dark conditions
glutathione
-
oxidized form, inhibition almost completely reversible by addition of reduced dithiothreitol
pyridoxal 5'-phosphate
-
inactivation is protected by ATP in combination with NADH
additional information
inhibited by addition of strong oxidants, reversible by addition of reducing agents
-
additional information
-
inhibited by addition of strong oxidants, reversible by addition of reducing agents
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
in light-adapted extracts, the presence or absence of reduced dithiothreitol has no significant effect on enzyme activity. However, the dark-adapted extracts incubated with reduced dithiothreitol exhibit a highly significant increase in enzyme activity
thioredoxin
-
reduced form, regulates activity via reversible reduction
thioredoxin
reduced form, regulates activity via reversible reduction, probably not relevant in vivo
thioredoxin
reduced form, regulates activity via reversible reduction
additional information
-
not activated by NAD+, NADP+, NADPH, reduced glutathione
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.096
D-ribulose 5-phosphate
-
wild-type enzyme, pH 8, 30°C
0.1
D-ribulose 5-phosphate
-
wild type enzyme, at 30°C, in 100 mM Tris-HCl (pH 8.2) containing 10 mM MgCl2, 0.5 mM dithiothreitol, 5 mM ATP, 0.2 mM phosphoenolpyruvate, 0.2 mM NADH, 2 units of pyruvate kinase, 2 units of lactic dehydrogenase, and 1 mM D-ribulose 5-phosphate
0.78
D-ribulose 5-phosphate
-
mutant enzyme H100A, at 30°C, in 100 mM Tris-HCl (pH 8.2) containing 10 mM MgCl2, 0.5 mM dithiothreitol, 5 mM ATP, 0.2 mM phosphoenolpyruvate, 0.2 mM NADH, 2 units of pyruvate kinase, 2 units of lactic dehydrogenase, and 1 mM D-ribulose 5-phosphate
1.35
D-ribulose 5-phosphate
-
mutant enzyme H100Q, at 30°C, in 100 mM Tris-HCl (pH 8.2) containing 10 mM MgCl2, 0.5 mM dithiothreitol, 5 mM ATP, 0.2 mM phosphoenolpyruvate, 0.2 mM NADH, 2 units of pyruvate kinase, 2 units of lactic dehydrogenase, and 1 mM D-ribulose 5-phosphate
1.37
D-ribulose 5-phosphate
-
mutant enzyme H100N, at 30°C, in 100 mM Tris-HCl (pH 8.2) containing 10 mM MgCl2, 0.5 mM dithiothreitol, 5 mM ATP, 0.2 mM phosphoenolpyruvate, 0.2 mM NADH, 2 units of pyruvate kinase, 2 units of lactic dehydrogenase, and 1 mM D-ribulose 5-phosphate
4
D-ribulose 5-phosphate
-
mutant enzyme Y98L, at 30°C, in 100 mM Tris-HCl (pH 8.2) containing 10 mM MgCl2, 0.5 mM dithiothreitol, 5 mM ATP, 0.2 mM phosphoenolpyruvate, 0.2 mM NADH, 2 units of pyruvate kinase, 2 units of lactic dehydrogenase, and 1 mM D-ribulose 5-phosphate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.22
6-phospho-D-gluconate
-
wild-type enzyme and S19A mutant, pH 8, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
410
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.9
8.4
8.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
less expressed in flower, and little or not expressed in root and silique
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
malfunction
metabolism
physiological function
malfunction
CP12 is a small, redox-sensitive protein. Arabidopsis CP12 mutants have reduced levels of phosphoribulokinase and impaired function of the Calvin-Benson cycle
malfunction
-
deletion of phosphoribulokinase results in proportional increases to both the H2 yield and the specific production rate
metabolism
-
heterologous expression of phosphoribulokinase (PrkA) or Rubisco perturbs the physiology of Escherichia coli by changing its internal energy balance and carbon flow, which are not favored for in situ CO2 recycling by the Rubisco-based engineered pathway. Both PrkA and Rubisco enhances the glycolysis through the Embden-Meyerhof-Parnas pathway
metabolism
A9W1C9
the Calvin cycle enzyme phosphoribulokinase is essential for growth on methanol
metabolism
phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis. The oxyphototrophic phosphoribulokinase (PRK) is redox-regulated and can be further regulated by reversible association with both glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and oxidized chloroplast protein CP12. The resulting GAPDH/CP12/PRK complex is central in the regulation of the Calvin-Benson-Bassham cycle
metabolism
-
in the absence of Rubisco, phosphoribulokinase negatively affects growth, and in turn, the H2 production rate
metabolism
phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis. The oxyphototrophic phosphoribulokinase (PRK) is redox-regulated and can be further regulated by reversible association with both glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and oxidized chloroplast protein CP12. The resulting GAPDH/CP12/PRK complex is central in the regulation of the Calvin-Benson-Bassham cycle
metabolism
-
phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis. The oxyphototrophic phosphoribulokinase (PRK) is redox-regulated and can be further regulated by reversible association with both glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and oxidized chloroplast protein CP12. The resulting GAPDH/CP12/PRK complex is central in the regulation of the Calvin-Benson-Bassham cycle
-
metabolism
-
the Calvin cycle enzyme phosphoribulokinase is essential for growth on methanol
-
physiological function
the enzyme strengthens the interaction between glyceraldehyde-3-phosphate dehydrogenase and chloroplast protein 12 within the supra-molecular complex
physiological function
phosphoribulokinase (PRK) is an essential enzyme of the Calvin-Benson-Bassham cycle in photosynthesis
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
200000 - 230000
-
sucrose densitiy gradient centrifugation, gel filtration, PAGE
230000
237000
252000 - 256000
-
sedimentation equilibrium centrifugation, gel filtration
33000
40000
41000
42000
44000
470000
-
high MW form, low speed sedimentation equilibrium centrifugation
48000
640000
-
glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase complex, gel filtration
82800 - 83000
82800 - 83000
-
low MW form, low speed sedimentation equilibrium centrifugation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodimer
multimer
octamer
tetramer
additional information
multimer
-
glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase complex, native form of enzyme with a molecular weight of 640000 Da
multimer
-
glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase complex, native form of enzyme
additional information
-
enzyme is part of a multienzymatic complex with glyeraldehyde-3-phosphate
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor diffusion method at 18°C, crystal structure of the enzyme in complex with glyceraldehyde-3-phosphate dehydrogenase and chloroplast protein CP12
sitting drop vapor diffusion method with NH4H2PO4 as precipitating agent
-
sitting-drop vapor diffusion method at 18°C, crystal structure of the enzyme in complex with ADP and glucose-6-phosphate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K165M
-
reduced catalytic activity, insensitive to inactivation by pyridoxal 5'-phosphate
R168Q
-
300fold decrease in catalytic efficiency, 50fold increased Km for D-ribulose 5-phosphate
S19A
-
ability to form complexes with Mg-ATP2-, decreased Vmax, increased Km for D-ribulose 5-phosphate
T18A
-
ability to form complexes with Mg-ATP2-, increased Km for D-ribulose 5-phosphate, decreased Vmax
C16S/C244S/C250S
-
triple mutant with altered oxidation-reduction midpoint potential as wild-type enzyme
C244S/C250S
-
double mutant with same oxidation-reduction midpoint potential as wild-type enzyme
additional information
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 10 mM bicine-KOH buffer, pH 7.8, 100 mM KCl, 5 mM dithiothreitol, several months
-
-80°C, 100 mM Tris buffer, pH 8.0, 0.5 mM dithiothreitol, 10% v/v glycerol
-
-80°C, N2-atmosphere, 50 mM bicine-KOH, 10 mM potassium phosphate, 10 mM dithiothreitol, 1 mM EDTA, 10% v/v glycerol, 2 months
-
0-4°C, 100 mM imidazole-HCl buffer, pH 7.0, 10 mM MgCl2, 1 mM EDTA, 1 mM dithioerythritol, 3 months
-
4°C, 0.02 M triethanolamine-HCl buffer, pH 7.6, 0.5 mM EDTA, 0.5 mM dithiothreitol, 4 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase complex
-
homogeneity
Sephadex G-50 column gel filtration and DEAE cellulose column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21(DE3) strain
heterologous expression of phosphoribulokinase (PrkA) or Rubisco perturbs the physiology of Escherichia coli by changing its internal energy balance and carbon flow, which are not favored for in situ CO2 recycling by the Rubisco-based engineered pathway. Both PrkA and Rubisco enhances the glycolysis through the Embden-Meyerhof-Parnas pathway
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cold acclimation does not alter the level of phosphoribulokinase mRNA or its enzyme activity
-
maximum expression of prk transcript is detected 6 h postillumination with 78.6fold increases. 2 h into the 12 h dark cycle, prk transcript level is still elevated 31.2fold
-
prk transcript levels decrease upon illumination (13.4fold by 2 h post-illumination) and by 1.5fold after 2 h dark. Enzyme activity decreases with increasing starvation time, though activity is still measureable after 6 months
-
the enzyme is downpregulated by dithiothreitol
the enzyme is downregulated by NADPH
the enzyme is not influenced by dithiothreitol
the enzyme is not influenced by dithiothreitol and NADPH
the enzyme is not influenced by NADPH
the enzyme is strongly upregulated by dithiothreitol
the enzyme is upregulated by dithiothreitol
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hurwitz, J.; Weissbach, A.; Horecker, B.L.; Smyrniotis, B.L.
Spinach phosphoribulokinase
J. Biol. Chem.
218
769-783
1956
Spinacia oleracea
brenda
Lin, M.; Turpin, D.H.
Purification and molecular and immunological characterization of a unique phosphoribulokinase from the green alga Selenastrum minutum
Plant Physiol.
98
82-88
1992
Monoraphidium minutum
brenda
Roesler, K.R.; Ogren, W.L.
Chlamydomonas reinhardtii phosphoribulokinase. Sequence, purification, and kinetics
Plant Physiol.
93
188-193
1990
Chlamydomonas reinhardtii
brenda
Serra, J.L.; Llama, M.J.; Rowell, P.; Stewart, W.D.P.
Purification and characterization of phosphoribulokinase from the N2-fixing cyanobacterium Anabaena cylindrica
Plant Sci.
59
1-9
1989
Anabaena cylindrica
-
brenda
Porter, M.A.; Milanez, S.; Stringer, C.D.; Hartman, F.C.
Purification and characterization of ribulose-5-phosphate kinase from spinach
Arch. Biochem. Biophys.
245
14-23
1986
Spinacia oleracea
brenda
Lazaro, J.J.; Sutton, C.W.; Nicholson, S.; Powls, R.
Characterisation of two forms of phosphoribulokinase isolated from the green alga, Scenedesmus obliquus
Eur. J. Biochem.
156
423-429
1986
Tetradesmus obliquus
brenda
Surek, B.; Heilbronn, A.; Austen, A.; Latzko, E.
Purification and characterization of phosphoribulokinase from wheat leaves
Planta
165
507-512
1985
Triticum aestivum
brenda
Rippel, S.; Bowien, B.
Phosphoribulokinase from Rhodospseudomonas acidophila
Arch. Microbiol.
139
207-212
1984
Rhodoblastus acidophilus, Rhodoblastus acidophilus 1150
-
brenda
Siebert, K.; Bowien, B.
Evidence for an octameric structure of phosphoribulokinase from Alcaligenes eutrophus
Biochim. Biophys. Acta
787
208-214
1984
Cupriavidus necator
-
brenda
Siebert, K.; Schobert, P.; Bowien, B.
Purification, some catalytic and molecular properties of phosphoribulokinase from Alcaligenes eutrophus
Biochim. Biophys. Acta
658
35-44
1981
Cupriavidus necator
brenda
Marsden, W.J.N.; Codd, G.A.
Purification and molecular and catalytic properties of phosphoribulokinase from the cyanobacterium Chlorogloeopsis fritschii
J. Gen. Microbiol.
130
999-1006
1984
Chlorogloeopsis fritschii
-
brenda
Berhow, M.A.; McFadden, B.A.
Ribulose 1,5-bisphosphate carboxylase and phosphoribulokinase in Prochloron
Planta
158
281-287
1983
Prochloron didemni
brenda
Tabita, F.R.
Pyridine nucleotide control and subunit structure of phosphoribulokinase from photosynthetic bacteria
J. Bacteriol.
143
1275-1280
1980
Rhodobacter capsulatus, Cereibacter sphaeroides, Rhodopseudomonas palustris, Rhodospirillum rubrum, Rhodocyclus tenuis, Magnetospirillum molischianum, Rhodomicrobium vannielii, Anabaena sp., Chlorella sorokiniana, Picosynechococcus sp. PCC 7002
brenda
Slabas, A.R.; Walker, D.A.
Inhibition of spinach phosphoribulokinase by DL-glyceraldehyde
Biochem. J.
153
613-619
1976
Spinacia oleracea
brenda
Abdelal, A.T.H.; Schlegel, H.G.
Separation of phosphoribulokinase from enzymes of the calvin cycle in Hydrogenomonas eutropha H 16
Arch. Microbiol.
95
139-143
1974
Cupriavidus necator
brenda
Abdelal, A.T.H.; Schlegel, H.G.
Purification and regulatory properties of phosphoribulokinase from Hydrogenomonas eutropha H 16
Biochem. J.
139
481-489
1974
Cupriavidus necator
brenda
MacElroy, R.D.; Mack, H.M.; Johnson, E.J.
Properties of phosphoribulokinase from Thiobacillus neapolitanus
J. Bacteriol.
112
532-538
1972
Halothiobacillus neapolitanus
brenda
Saharan, M.M.R.; Singh, R.
Purification and characterization of phosphoribulokinase from immature pods of Brassica
J. Plant Biochem. Biotechnol.
2
121-124
1993
Brassica sp.
-
brenda
Lavergne, D.; Bismuth, E.
Simultaneous purification of two kinases from spinach leaves
Plant Sci. Lett.
1
229-236
1973
Spinacia oleracea
-
brenda
Kagawa, T.
Isolation and purification of ribulose-5-phosphate kinase from Nicotiana glutinosa
Methods in Chloroplast and Molecular Biology (Edelman, M. , Hallick, R. B. , Chua, M. eds.) Elsevier Biomedical Press
695-705
1982
Nicotiana glutinosa
-
brenda
Krieger, T.J.; Miziorko, H.M.
Spinach leaf ribulose-5-phosphate kinase: examination of sulfhydryls by chemical modification and spin-labeling
Arch. Biochem. Biophys.
256
362-371
1987
Spinacia oleracea
brenda
Joint, I.R.; Morris, I.; Fuller, R.C.
Purification of a complex of alkaline fructose 1,6-bisphosphatase and phosphoribulokinase from Rhodospirillum rubrum
J. Biol. Chem.
247
4833-4838
1972
Rhodospirillum rubrum
brenda
Kiesow, L.A.; Lindsley, B.F.; Bless, J.W.
Phosphoribulokinase from Nitrobacter winogradskyi: activation by reduced nicotinamide adenine dinucleotide and inhibition by pyridoxal phosphate
J. Bacteriol.
130
20-25
1977
Nitrobacter winogradskyi
brenda
Hart, B.A.; Gibson, J.
Ribulose-5-phosphate kinase from Chromatium sp. strain D
Arch. Biochem. Biophys.
144
308-321
1971
Chromatium sp., Chromatium sp. D
brenda
Hirasawa, M.; Brandes, H.K.; Hartman, F.C.; Knaff, D.B.
Oxidation-reduction properties of the regulatory site of spinach phosphoribulokinase
Arch. Biochem. Biophys.
350
127-131
1998
Spinacia oleracea
brenda
Harrison, D.H.; Runquist, J.A.; Holub, A.; Miziorko, H.M.
The crystal structure of phosphoribulokinase from Rhodobacter sphaeroides reveals a fold similar to that of adenylate kinase
Biochemistry
37
5074-5085
1998
Cereibacter sphaeroides
brenda
Runquist, J.A.; Narasimhan, C.; Wolff, C.E.; Koteiche, H.A.; Miziorko, H.M.
Rhodobacter sphaeroides phosphoribulokinase: binary and ternary complexes with nucleotide substrate analogs and effectors
Biochemistry
35
15049-15056
1996
Cereibacter sphaeroides
brenda
Roberts, D.L.; Runquist, J.A.; Miziorko, H.M.; Kim, J.J.
Crystallization and preliminary X-ray crystallographic analysis of phosphoribulokinase from Rhodobacter sphaeroides
Protein Sci.
4
2442-2443
1995
Cereibacter sphaeroides
brenda
Wadano, A.; Kamata, Y.; Iwaki, T.; Nishikawa, K.; Hirahashi, T.
Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942
Plant Cell Physiol.
36
1381-1385
1995
Synechococcus sp., Synechococcus sp. PCC 7942
brenda
Avilan, L.; Lebreton, S.; Gontero, B.
Thioredoxin activation of phosphoribulokinase in a bi-enzyme complex from Chlamydomonas reinhardtii chloroplasts
J. Biol. Chem.
275
9447-9451
2000
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii WM3-
brenda
Geck, M.K.; Hartman, F.C.
Kinetic and mutational analyses of the regulation of phosphoribulokinase by thioredoxins
J. Biol. Chem.
275
18034-18039
2000
Spinacia oleracea
brenda
Hariharan, T.; Johnson, P.J.; Cattolico, R.A.
Purification and characterization of phosphoribulokinase from the marine chromophytic alga Heterosigma carterae
Plant Physiol.
117
321-329
1998
Heterosigma akashiwo
brenda
Koyabashi, D.; Tamoi, M.; Iwaki, T.; Shigeoka, S; Wadano, A.
Molecular characterization and redox regulation of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 7942
Plant Cell Physiol.
44
269-276
2003
Synechococcus sp., Synechococcus sp. PCC 7942
brenda
Miziorko, H.M.
Phosphoribulokinase: current perspectives on the structure/function basis for regulation and catalysis
Adv. Enzymol. Relat. Areas Mol. Biol.
74
95-127
2000
Spinacia oleracea, Chlamydomonas reinhardtii, Rhodoblastus acidophilus, Chlorogloeopsis fritschii, Rhodobacter capsulatus, Cereibacter sphaeroides, Halothiobacillus neapolitanus, Nitrobacter winogradskyi, Heterosigma akashiwo, Cupriavidus necator, Acidovorax facilis
brenda
Mouche, F.; Gontero, B.; Callebaut, I.; Mornon, J.P.; Boisset, N.
Striking conformational change suspected within the phosphoribulokinase dimer induced by interaction with GAPDH
J. Biol. Chem.
277
6743-6749
2002
Chlamydomonas reinhardtii
brenda
Runquist, J.A.; Harrison, D.H.T.; Miziorko, H.M.
Rhodobacter sphaeroides phosphoribulokinase: identification of lysine-165 as a catalytic residue and evaluation of the contributions of invariant basic amino acids to ribulose 5-phosphate binding
Biochemistry
38
13999-14005
1999
Cereibacter sphaeroides
brenda
Runquist, J.A.; Rios, S.E.; Vinarov, D.A.; Miziorko, H.M.
Functional evaluation of serine/threonine residues in the P-loop of Rhodobacter sphaeroides phosphoribulokinase
Biochemistry
400
14530-14537
2001
Cereibacter sphaeroides
brenda
Wadano, A.; Nishikawa, K.; Hirashi, T.; Satoh, R.; Kwaki, T.
Reaction mechanism of phosphoribulokinase from a cyanobacterium, Synechococcus PCC7942
Photosynth. Res.
56
27-33
1998
Synechococcus sp.
-
brenda
Runquist, J.A.; Harrison, D.H.; Miziorko, H.M.
Functional evaluation of invariant arginines situated in the mobile lid domain of phosphoribulokinase
Biochemistry
37
1221-1226
1998
Cereibacter sphaeroides
brenda
Marri, L.; Sparla, F.; Pupillo, P.; Trost, P.
Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana
J. Exp. Bot.
56
73-80
2005
Arabidopsis thaliana
brenda
Dani, D.N.; Sainis, J.K.
Isolation and characterization of a thylakoid membrane module showing partial light and dark reactions
Biochim. Biophys. Acta
1669
43-52
2005
Synechococcus elongatus PCC 7942 = FACHB-805
brenda
Lebreton, S.; Graciet, E.; Gontero, B.
Modulation, via protein-protein interactions, of glyceraldehyde-3-phosphate dehydrogenase activity through redox phosphoribulokinase regulation
J. Biol. Chem.
278
12078-12084
2003
Chlamydomonas reinhardtii
brenda
Michels, A.K.; Wedel, N.; Kroth, P.G.
Diatom plastids possess a phosphoribulokinase with an altered regulation and no oxidative pentose phosphate pathway
Plant Physiol.
137
911-920
2005
Trieres chinensis (Q95033), Trieres chinensis, Spinacia oleracea (P09559), Spinacia oleracea
brenda
Marri, L.; Trost, P.; Pupillo, P.; Sparla, F.
Reconstitution and properties of the recombinant glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase supramolecular complex of Arabidopsis
Plant Physiol.
139
1433-1443
2005
Arabidopsis thaliana
brenda
Petersen, J.; Teich, R.; Brinkmann, H.; Cerff, R.
A "green" phosphoribulokinase in complex algae with red plastids: evidence for a single secondary endosymbiosis leading to haptophytes, cryptophytes, heterokonts, and dinoflagellates
J. Mol. Evol.
62
143-157
2006
Chondrus crispus (Q24LS9), Prymnesium parvum (Q24LS8), Diacronema lutheri (Q24LT5), Euglena gracilis (Q24LT0), Guillardia theta (Q24LT4), Lingulaulax polyedra (Q24LT3), Pyrocystis lunula, Diacronema lutheri 926-1 (Q24LT5), Prymnesium parvum 127.79 (Q24LS8)
brenda
Anderson, L.E.; Chrostowski, J.; Carol, A.A.
Enzyme co-localization with transketolase, xylulose-5-P 3-epimerase and phosphoriboisomerase in pea leaf chloroplasts
Plant Sci.
171
686-698
2006
Lathyrus oleraceus
-
brenda
Runquist, J.A.; Miziorko, H.M.
Functional contribution of a conserved, mobile loop histidine of phosphoribulokinase
Protein Sci.
15
837-842
2006
Cereibacter sphaeroides
brenda
Babadzhanova, M.P.; Babadzhanova, M.A.; Aliev, K.A.
Developmental changes in the activities of enzymes of free multienzyme complexes involved in the Benson-Calvin cycle
Russ. J. Plant Physiol.
53
32-38
2006
Gossypium hirsutum
-
brenda
Erales, J.; Avilan, L.; Lebreton, S.; Gontero, B.
Exploring CP12 binding proteins revealed aldolase as a new partner for the phosphoribulokinase/glyceraldehyde 3-phosphate dehydrogenase/CP12 complex--purification and kinetic characterization of this enzyme from Chlamydomonas reinhardtii
FEBS J.
275
1248-1259
2008
Chlamydomonas reinhardtii
brenda
Swingley, W.D.; Sadekar, S.; Mastrian, S.D.; Matthies, H.J.; Hao J.; Ramos, H.; Acharya, C.R.; Conrad, A.L.; Taylor, H.L.; Dejesa, L.C.; Shah, M.K.; O'huallachain, M.E.; Lince, M.T.; Blankenship, R.E.; Beatty, J.T.; Touchman, J.W.
The complete genome sequence of Roseobacter denitrificans reveals a mixotrophic rather than photosynthetic metabolism
J. Bacteriol.
189
683-690
2007
no activity in Roseobacter denitrificans OCh 114
brenda
Maberly, S.C.; Courcelle, C.; Groben, R.; Gontero, B.
Phylogenetically-based variation in the regulation of the Calvin cycle enzymes, phosphoribulokinase and glyceraldehyde-3-phosphate dehydrogenase, in algae
J. Exp. Bot.
61
735-745
2009
Fistulifera pelliculosa, Thalassiosira pseudonana, Pseudocharaciopsis ovalis, Bumilleriopsis peterseniana, Mallomonas caudata, Dinobryon sociale, Emiliania huxleyi, Hemiselmis rufescens, Euglena gracilis, Staurastrum cingulum, Chlamydomonas reinhardtii, Porphyridium purpureum, Cyanophora paradoxa, Alexandrium minutum, Asterionella formosa, Aulacoseira granulata, Asterionella formosa 19, Asterionella formosa 18
brenda
Rumpho, M.E.; Pochareddy, S.; Worful, J.M.; Summer, E.J.; Bhattacharya, D.; Pelletreau, K.N.; Tyler, M.S.; Lee, J.; Manhart, J.R.; Soule, K.M.
Molecular characterization of the calvin cycle enzyme phosphoribulokinase in the stramenopile alga Vaucheria litorea and the plastid hosting mollusc Elysia chlorotica
Mol. Plant
2
1384-1396
2009
Vaucheria litorea (Q9ATC3), Vaucheria litorea
brenda
Marri, L.; Zaffagnini, M.; Collin, V.; Issakidis-Bourguet, E.; Lemaire, S.D.; Pupillo, P.; Sparla, F.; Miginiac-Maslow, M.; Trost, P.
Prompt and easy activation by specific thioredoxins of calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex
Mol. Plant
2
259-269
2009
Arabidopsis thaliana
brenda
Kane, K.; Moheb, A.; Fukushi, Y.; Roy, R.; Huener, N.P.; Ibrahim, R.K.; Sarhan, F.
Daphnetin methylation stabilizes the activity of phosphoribulokinase in wheat during cold acclimation
Biochem. Cell Biol.
90
657-666
2012
Triticum aestivum
brenda
Soule, K.; Rumpho, M.
Light-regulated photosynthetic gene expression and phosphoribulokinase enzyme activity in the heterokont alga Vaucheria litorea (Xanthophyceae) and its symbiotic molluskan partner Elysia chlorotica (Gastropoda)
J. Phycol.
48
373-383
2012
Elysia chlorotica, Vaucheria litorea
brenda
Avilan, L.; Puppo, C.; Erales, J.; Woudstra, M.; Lebrun, R.; Gontero, B.
CP12 residues involved in the formation and regulation of the glyceraldehyde-3-phosphate dehydrogenase-CP12-phosphoribulokinase complex in Chlamydomonas reinhardtii
Mol. Biosyst.
8
2994-3002
2012
Chlamydomonas reinhardtii (A8IYP4), Chlamydomonas reinhardtii
brenda
Wilson, R.H.; Hayer-Hartl, M.; Bracher, A.
Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301
Acta Crystallogr. Sect. F
75
278-289
2019
Synechococcus elongatus PCC 6301 (A0A0H3K6J7), Synechococcus elongatus PCC 6301
brenda
Ochsner, A.M.; Christen, M.; Hemmerle, L.; Peyraud, R.; Christen, B.; Vorholt, J.A.
Transposon sequencing uncovers an essential regulatory function of phosphoribulokinase for methylotrophy
Curr. Biol.
27
2579-2588
2017
Methylorubrum extorquens (A9W1C9), Methylorubrum extorquens PA1 (A9W1C9), Methylorubrum extorquens PA1
brenda
McCully, A.; McKinlay, J.
Disrupting Calvin cycle phosphoribulokinase activity in Rhodopseudomonas palustris increases the H2 yield and specific production rate proportionately
Int. J. Hydrogen Energy
41
4143-4149
2016
Rhodopseudomonas palustris
-
brenda
Elena Lopez-Calcagno, P.; Omar Abuzaid, A.; Lawson, T.; Anne Raines, C.
Arabidopsis CP12 mutants have reduced levels of phosphoribulokinase and impaired function of the Calvin-Benson cycle
J. Exp. Bot.
68
2285-2298
2017
Arabidopsis thaliana (P25697), Arabidopsis thaliana
brenda
Liu, E.J.; Tseng, I.T.; Chen, Y.L.; Pang, J.J.; Shen, Z.X.; Li, S.Y.
The physiological responses of Escherichia coli triggered by phosphoribulokinase (PrkA) and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco)
Microorganisms
8
1187
2020
Escherichia coli
brenda
Yu, A.; Xie, Y.; Pan, X.; Zhang, H.; Cao, P.; Su, X.; Chang, W.; Li, M.
Photosynthetic phosphoribulokinase structures enzymatic mechanisms and the redox regulation of the Calvin-Benson-Bassham cycle
Plant Cell
32
1556-1573
2020
Synechococcus elongatus (Q31PL2), Arabidopsis thaliana (P25697), Arabidopsis thaliana, Synechococcus elongatus PCC 7942 (Q31PL2)
brenda
McFarlane, C.R.; Shah, N.R.; Kabasakal, B.V.; Echeverria, B.; Cotton, C.A.R.; Bubeck, D.; Murray, J.W.
Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria
Proc. Natl. Acad. Sci. USA
116
20984-20990
2019
Thermosynechococcus vestitus (Q8DHN2)
brenda
Gurrieri, L.; Del Giudice, A.; Demitri, N.; Falini, G.; Pavel, N.V.; Zaffagnini, M.; Polentarutti, M.; Crozet, P.; Marchand, C.H.; Henri, J.; Trost, P.; Lemaire, S.D.; Sparla, F.; Fermani, S.
Arabidopsis and Chlamydomonas phosphoribulokinase crystal structures complete the redox structural proteome of the Calvin-Benson cycle
Proc. Natl. Acad. Sci. USA
116
8048-8053
2019
Chlamydomonas reinhardtii (P19824), Chlamydomonas reinhardtii, Arabidopsis thaliana (P25697), Arabidopsis thaliana
brenda
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