Any feedback?
Information on EC 3.1.3.37 - sedoheptulose-bisphosphatase
for references in articles please use BRENDA:EC3.1.3.37Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.3.37 sedoheptulose-bisphosphataseSpecify your search results
Word Map
- 3.1.3.37
- chloroplast
-
calvin
- rubisco
- ribulose-1,5-bisphosphate
- phosphoribulokinase
- rubp
-
calvin-benson
-
calvin-benson-bassham
-
glyceraldehyde-3-p
- biofuel production
- biotechnology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
sbpase, sedoheptulose-1,7-bisphosphatase, sedoheptulose bisphosphatase, fbp/sbpase, sedoheptulose 1,7-bisphosphatase, fructose-1,6-/sedoheptulose-1,7-bisphosphatase, fructose-1,6/sedoheptulose-1,7-bisphosphatase, sed(1,7)p2ase, sedoheptulose-bisphosphatase, sebp1, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BiBPase
bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase
dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase
Thermosynechococcus vestitus
-
FBP/SBPase
fructose -1,6-/sedoheptulose-1,7-bisphosphatase
fructose-1,6-biphosphatase/sedoheptulose-1,7-biphosphatase
-
bifunctional enzyme, F-I
fructose-1,6/sedoheptulose-1,7-bisphosphatase
GlpXp
-
bifunctional enzyme with sedoheptulose 1,7-bisphosphatase and fructose 1,6-bisphosphatase activities
ore
phosphatase, sedoheptulose di-
-
-
-
-
SBPase
SebP1
SED(1,7)P2ASE
-
-
-
-
sedoheptulose 1,7-bisphosphatase
sedoheptulose 1,7-diphosphatase
-
-
-
-
sedoheptulose 1,7-diphosphate phosphatase
-
-
-
-
sedoheptulose bisphosphatase
sedoheptulose diphosphatase
-
-
-
-
sedoheptulose-1,7-bisphosphatase
Sedoheptulose-bisphosphatase
-
-
-
-
SedP2-ase
-
-
-
-
SYNPCC7002_A1301
bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase
-
bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase
Synechococcus sp. PCC 7002 ATCC 27264
-
-
bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase
Synechococcus sp. PCC 7002 PR-6
-
-
fructose -1,6-/sedoheptulose-1,7-bisphosphatase
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
SBPase
-
-
-
-
sedoheptulose 1,7-bisphosphatase
-
-
-
-
sedoheptulose bisphosphatase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-1,7-bisphosphate 1-phosphohydrolase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9055-32-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
15% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
Fructose 1-phosphate + H2O
Fructose + phosphate
-
11% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
glucose 1,6-diphosphate + H2O
phosphate + ?
-
11% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
-
5.5% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
ribulose 1,5-diphosphate + H2O
phosphate + ?
-
5.5% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
fructose 1,6-bisphosphate + H2O
phosphate + ?
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
fructose 1,6-bisphosphate + H2O
phosphate + ?
-
22% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
fructose 1,6-bisphosphate + H2O
phosphate + ?
-
about 20-25% of the activity obtained with seduheptulose 1,7-bisphosphate
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
the enzyme is involved in the generation of CO2-acceptor ribulose 1,5-bisphosphate in the Calvin cycle
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
the enzyme is involved photosynthetic CO2 fixation
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
the enzyme is involved in the generation of CO2-acceptor ribulose 1,5-bisphosphate in the Calvin cycle
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
the enzyme is involved photosynthetic CO2 fixation via generation of CO2-acceptor ribulose 1,5-bisphosphate in the Calvin cycle
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
the enzyme is involved photosynthetic CO2 fixation
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
some enzymes involved in the fixation of CO2, i.e. glyceraldehyde 3-dehydrogenase, triose phosphate isomerase, aldolase, and seduheptulose bisphosphatase, are co-localized in the chloroplast stroma for direct transfer of substrate/products from one enzyme to another, while the fructose bisphosphatase is not co-localized, overview
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
134828, 134829, 134830, 134834, 134837, 134838, 134839, 134840, 134841, 134844, 134846, 134847, 134848
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
Synechococcus sp. PCC 7002 ATCC 27264
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
Synechococcus sp. PCC 7002 PR-6
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
Thermosynechococcus vestitus
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
specific for
-
-
?
additional information
?
-
-
the enzyme of the pentose-phosphate pathway is encoded by a light-regulated gene
-
-
?
additional information
?
-
-
involved in photosynthetic carbon fixation
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
Calvin cycle enzyme
-
-
?
additional information
?
-
-
the enzyme is interconverted from an inactive to an active form when a plant is illuminated
-
-
?
additional information
?
-
-
the enzyme is involved in the reductive pentose phosphate cycle. Light activation of the enzyme in intact seedlings
-
-
?
additional information
?
-
-
appearance of sedoheptulose 1,7-diphosphatase activity on conversion of chloroplast fructose 1,6-diphosphatase from dimeric form to monomeric enzyme form
-
-
?
additional information
?
-
-
chloroplasts have the ability to inactivate the three Calvin cycle enzymes, fructose 1,6-diphosphatase, sedoheptulose 1,7-diphosphatase and ribulose 5-phosphate kinase, virtually completely in the dark phase by a combined effect of changes of the reductive state of the electron-transport carrier on all three enzymes, changes of stromal Mg2+ and and pH on fructose 1,6-bisphosphatase and sedoheptulose 1,7-bisphosphatase and changes of stromal ATP/ADP ratios on ribulose 5-phosphate kinase
-
-
?
additional information
?
-
-
regulatory enzyme whose activity in chloroplasts is controlled via ferredoxin by light
-
-
?
additional information
?
-
-
involved in photosynthetic carbon fixation
-
-
?
additional information
?
-
Thermosynechococcus vestitus
a dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) exhibiting activity of EC 3.1.3.37, sedoheptulose 1,7-diphosphatase, and 3.1.3.11, fructose 1,6-bisphosphatase
-
-
?
additional information
?
-
-
enzyme has a key role in regulating the photosynthetic Calvin cycle
-
-
?
additional information
?
-
-
one of several enzymes of the reductive pentose phosphate pathway
-
-
?
additional information
?
-
-
under conditions that are likely to obtain in the stroma in the dark, the model predicts that approximately 99.1% of the enzyme will be in the inactive oxidized forms. Such inactivation is important since it will prevent the reductive pentose phosphate pathway from operating in darkness
-
-
?
additional information
?
-
-
involved in photosynthetic carbon fixation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
the enzyme is involved in the generation of CO2-acceptor ribulose 1,5-bisphosphate in the Calvin cycle
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
the enzyme is involved photosynthetic CO2 fixation
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
the enzyme is involved in the generation of CO2-acceptor ribulose 1,5-bisphosphate in the Calvin cycle
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
the enzyme is involved photosynthetic CO2 fixation via generation of CO2-acceptor ribulose 1,5-bisphosphate in the Calvin cycle
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
the enzyme is involved photosynthetic CO2 fixation
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
some enzymes involved in the fixation of CO2, i.e. glyceraldehyde 3-dehydrogenase, triose phosphate isomerase, aldolase, and seduheptulose bisphosphatase, are co-localized in the chloroplast stroma for direct transfer of substrate/products from one enzyme to another, while the fructose bisphosphatase is not co-localized, overview
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
Synechococcus sp. PCC 7002 ATCC 27264
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
Synechococcus sp. PCC 7002 PR-6
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
Thermosynechococcus vestitus
-
-
-
?
additional information
?
-
-
the enzyme of the pentose-phosphate pathway is encoded by a light-regulated gene
-
-
?
additional information
?
-
-
involved in photosynthetic carbon fixation
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
Calvin cycle enzyme
-
-
?
additional information
?
-
-
the enzyme is interconverted from an inactive to an active form when a plant is illuminated
-
-
?
additional information
?
-
-
the enzyme is involved in the reductive pentose phosphate cycle. Light activation of the enzyme in intact seedlings
-
-
?
additional information
?
-
-
chloroplasts have the ability to inactivate the three Calvin cycle enzymes, fructose 1,6-diphosphatase, sedoheptulose 1,7-diphosphatase and ribulose 5-phosphate kinase, virtually completely in the dark phase by a combined effect of changes of the reductive state of the electron-transport carrier on all three enzymes, changes of stromal Mg2+ and and pH on fructose 1,6-bisphosphatase and sedoheptulose 1,7-bisphosphatase and changes of stromal ATP/ADP ratios on ribulose 5-phosphate kinase
-
-
?
additional information
?
-
-
regulatory enzyme whose activity in chloroplasts is controlled via ferredoxin by light
-
-
?
additional information
?
-
-
involved in photosynthetic carbon fixation
-
-
?
additional information
?
-
Thermosynechococcus vestitus
a dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) exhibiting activity of EC 3.1.3.37, sedoheptulose 1,7-diphosphatase, and 3.1.3.11, fructose 1,6-bisphosphatase
-
-
?
additional information
?
-
-
enzyme has a key role in regulating the photosynthetic Calvin cycle
-
-
?
additional information
?
-
-
one of several enzymes of the reductive pentose phosphate pathway
-
-
?
additional information
?
-
-
under conditions that are likely to obtain in the stroma in the dark, the model predicts that approximately 99.1% of the enzyme will be in the inactive oxidized forms. Such inactivation is important since it will prevent the reductive pentose phosphate pathway from operating in darkness
-
-
?
additional information
?
-
-
involved in photosynthetic carbon fixation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-hydroxy-N'-((6-methyl-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
2-methyl-N'-((6-methyl-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
2-[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]-N'-[(E)-(4-methylphenyl)methylidene]acetohydrazide
-
2-[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]-N'-[(E)-(5-hydroxy-2-methylphenyl)methylidene]acetohydrazide
-
2-[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]-N-(2,3-dihydro-1H-inden-5-yl)acetamide
-
2-[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]-N-(2,6-dimethylphenyl)acetamide
-
2-[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]-N-(3-fluoro-4-methylphenyl)acetamide
-
2-[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]-N-(3-oxo-1,3-dihydro-2-benzofuran-5-yl)acetamide
-
3-bromo-N'-((6-(tert-butyl)-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
3-bromo-N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
3-bromo-N'-((6-chloro-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
3-bromo-N'-((6-ethyl-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
3-bromo-N'-((6-fluoro-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
3-bromo-N'-((6-hydroxy-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
3-bromo-N'-((6-isopropyl-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
3-bromo-N'-((6-methyl-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
3-bromo-N'-((6-nitro-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
4-bromo-N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
methyl 4-([[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]acetyl]amino)benzoate
-
N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)-4-(trifluoromethyl)benzohydrazide
-
N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)-4-fluorobenzohydrazide
-
N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)-4-hydroxybenzohydrazide
-
N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)-4-methylbenzohydrazide
-
N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)-4-nitrobenzohydrazide
-
oxidized thioredoxin f
-
due to the formation of a stable complex between enzyme and thioredoxin
-
AMP
Thermosynechococcus vestitus
a regulatory inhibitor, AMP-binding loop structure analysis
Ca2+
-
2 mM, at pH 8.0, 83% inhibition of the thiol-treated enzyme, at pH 7.5 91% inhibition and at pH 7.0 complete inhibition
additional information
-
location of the redox-active cysteines in chloroplast sedoheptulose-1,7-bisphosphatase indicates that its allosteric regulation is similar but not identical to that of fructose 1,6-bisphosphatase
-
additional information
-
location of the redox-active cysteines in chloroplast sedoheptulose-1,7-bisphosphatase indicates that its allosteric regulation is similar but not identical to that of fructose 1,6-bisphosphatase
-
additional information
-
location of the redox-active cysteines in chloroplast sedoheptulose-1,7-bisphosphatase indicates that its allosteric regulation is similar but not identical to that of fructose 1,6-bisphosphatase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Dithiol
-
absolute requirement for a dithiol at pH values below pH 7.7, i.e. reduced thioredoxin f or dithiothreitol
dithiothreitol
-
activation is strongly impaired by incubating oxidized enzyme in the presence of Fe2+ before addition of dithiothreitol
additional information
-
location of the redox-active cysteines in chloroplast sedoheptulose-1,7-bisphosphatase indicates that its allosteric regulation is similar but not identical to that of fructose 1,6-bisphosphatase
-
additional information
-
there is a strong positive correlation between in vivo and in vitro SBPase activity in high light and moderate or high CO2 but not when light or CO2 fluxes are low
-
additional information
-
location of the redox-active cysteines in chloroplast sedoheptulose-1,7-bisphosphatase indicates that its allosteric regulation is similar but not identical to that of fructose 1,6-bisphosphatase
-
additional information
-
location of the redox-active cysteines in chloroplast sedoheptulose-1,7-bisphosphatase indicates that its allosteric regulation is similar but not identical to that of fructose 1,6-bisphosphatase
-