Information on EC 3.1.3.37 - sedoheptulose-bisphosphatase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.1.3.37
-
RECOMMENDED NAME
GeneOntology No.
sedoheptulose-bisphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Calvin-Benson-Bassham cycle
-
Carbon fixation in photosynthetic organisms
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-1,7-bisphosphate 1-phosphohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
FBPase/SBPase
-
-
fructose -1,6-/sedoheptulose-1,7-bisphosphatase
-
-
fructose-1,6-biphosphatase/sedoheptulose-1,7-biphosphatase
-
bifunctional enzyme, F-I
phosphatase, sedoheptulose di-
-
-
-
-
SBPase
-
-
-
-
SBPase
C4PAW8
-
SBPase
Cucumis sativus Jinyou 3
C4PAW8
-
-
SBPase
Synechococcus sp. PCC7942
-
-
-
SED(1,7)P2ASE
-
-
-
-
sedoheptulose 1,7-bisphosphatase
-
-
-
-
sedoheptulose 1,7-diphosphatase
-
-
-
-
sedoheptulose 1,7-diphosphate phosphatase
-
-
-
-
sedoheptulose bisphosphatase
-
-
-
-
sedoheptulose bisphosphatase
-
-
sedoheptulose diphosphatase
-
-
-
-
sedoheptulose-1,7-bisphosphatase
-
-
sedoheptulose-1,7-bisphosphatase
-
-
sedoheptulose-1,7-bisphosphatase
C4PAW8
-
sedoheptulose-1,7-bisphosphatase
Cucumis sativus Jinyou 3
C4PAW8
-
-
sedoheptulose-1,7-bisphosphatase
A8DUA7
-
sedoheptulose-1,7-bisphosphatase
-
-
sedoheptulose-1,7-bisphosphatase
-
-
sedoheptulose-1,7-bisphosphatase
-
-
sedoheptulose-1,7-bisphosphatase
-
-
sedoheptulose-1,7-bisphosphatase
-
-
sedoheptulose-1,7-bisphosphatase
Synechococcus sp. PCC7942
-
-
-
sedoheptulose-1,7-bisphosphatase
-
-
sedoheptulose-1-7 bisphosphatase
-
-
Sedoheptulose-bisphosphatase
-
-
-
-
SedP2-ase
-
-
-
-
seduheptulose bisphosphatase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9055-32-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene CsSBP
UniProt
Manually annotated by BRENDA team
Cucumis sativus Jinyou 3
gene CsSBP
UniProt
Manually annotated by BRENDA team
strain H16
-
-
Manually annotated by BRENDA team
cultivar Samsun
-
-
Manually annotated by BRENDA team
wild type and antisense transgenic plants
-
-
Manually annotated by BRENDA team
subspecies Oryza sativa indica, cultivar 9311
-
-
Manually annotated by BRENDA team
var. Little Marvel
-
-
Manually annotated by BRENDA team
variant Little Marvel
-
-
Manually annotated by BRENDA team
overexpression in Nicotiana tabacum
-
-
Manually annotated by BRENDA team
strain PCC 7942, bifunctional fructose-1,6/seduheptulose-1,7-bisphosphatase
-
-
Manually annotated by BRENDA team
strain PCC 7942, FBPase-I, isoform with enzymic activity
-
-
Manually annotated by BRENDA team
strain PCC7942
-
-
Manually annotated by BRENDA team
Synechococcus sp. PCC7942
strain PCC7942
-
-
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
C4PAW8
Sedoheptulose-1,7-bisphosphatase is a key enzyme in the photosynthetic carbon reduction cycle, i.e. Calvin cycle
physiological function
-
the C3 cycle enzyme sedoheptulose-1,7 bisphosphatase exerts strong metabolic control over ribulose-5-phosphate regeneration at light saturation
metabolism
Cucumis sativus Jinyou 3
-
Sedoheptulose-1,7-bisphosphatase is a key enzyme in the photosynthetic carbon reduction cycle, i.e. Calvin cycle
-
additional information
-
enzyme-overexpressing Nicotiana tabacum plants show greater carbon assimilation and electron transport rates compared to non-transfected plants, phenotype, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
15% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
fructose 1,6-bisphosphate + H2O
phosphate + ?
show the reaction diagram
-
-
-
-
?
fructose 1,6-bisphosphate + H2O
phosphate + ?
show the reaction diagram
-
-
-
-
?
fructose 1,6-bisphosphate + H2O
phosphate + ?
show the reaction diagram
-
22% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
fructose 1,6-bisphosphate + H2O
phosphate + ?
show the reaction diagram
-
about 20-25% of the activity obtained with seduheptulose 1,7-bisphosphate
-
?
Fructose 1-phosphate + H2O
Fructose + phosphate
show the reaction diagram
-
11% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
glucose 1,6-diphosphate + H2O
phosphate + ?
show the reaction diagram
-
11% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
ribulose 1,5-diphosphate + H2O
phosphate + ?
show the reaction diagram
-
5.5% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
specific for
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved photosynthetic CO2 fixation
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
the enzyme is involved photosynthetic CO2 fixation
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
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
show the reaction diagram
Synechococcus sp. PCC7942
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphatase + phosphate
show the reaction diagram
Cucumis sativus, Cucumis sativus Jinyou 3
C4PAW8
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
5.5% of the activity with sedoheptulose 1,7-diphosphate
-
-
?
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
?
-
-
Calvin cycle enzyme
-
-
-
additional information
?
-
-
Calvin cycle enzyme
-
-
-
additional information
?
-
-
Calvin cycle enzyme
-
-
-
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
?
-
-
enzyme has a key role in regulating the photosynthetic Calvin cycle
-
-
-
additional information
?
-
-
regulatory enzyme whose activity in chloroplasts is controlled via ferredoxin by light
-
-
-
additional information
?
-
-
the enzyme is interconverted from an inactive to an active form when a plant is illuminated
-
-
-
additional information
?
-
-
the enzyme of the pentose-phosphate pathway is encoded by a light-regulated gene
-
-
-
additional information
?
-
-
one of several enzymes of the reductive pentose phosphate pathway
-
-
-
additional information
?
-
-
the enzyme is involved in the reductive pentose phosphate cycle. Light activation of the enzyme in intact seedlings
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved photosynthetic CO2 fixation
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
the enzyme is involved photosynthetic CO2 fixation
-
-
ir
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
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-phosphatase + phosphate
show the reaction diagram
Cucumis sativus, Cucumis sativus Jinyou 3
C4PAW8
-
-
-
?
additional information
?
-
-
Calvin cycle enzyme
-
-
-
additional information
?
-
-
Calvin cycle enzyme
-
-
-
additional information
?
-
-
Calvin cycle enzyme
-
-
-
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
?
-
-
enzyme has a key role in regulating the photosynthetic Calvin cycle
-
-
-
additional information
?
-
-
regulatory enzyme whose activity in chloroplasts is controlled via ferredoxin by light
-
-
-
additional information
?
-
-
the enzyme is interconverted from an inactive to an active form when a plant is illuminated
-
-
-
additional information
?
-
-
the enzyme of the pentose-phosphate pathway is encoded by a light-regulated gene
-
-
-
additional information
?
-
-
one of several enzymes of the reductive pentose phosphate pathway
-
-
-
additional information
?
-
-
the enzyme is involved in the reductive pentose phosphate cycle. Light activation of the enzyme in intact seedlings
-
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activation
Mg2+
-
no requirement
Mg2+
-
5 mM required for maximal activity
Mg2+
-
required
Mg2+
-
required
Mg2+
-
no activation in absence of a dithiol reductant; required
Mg2+
-
required, optimal at 15 mM
Mn2+
-
can partially replace Mg2+ in activation
additional information
-
no requirement for divalent cation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acrolein
-
treatment of intact chloroplast
Ca2+
-
0.7 mM, 50% inhibition
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
Cu2+
-
0.1 mM, 30% inhibition
dehydroascorbate
-
-
fructose 1,6-diphosphate
-
at high concentrations
NaCl
-
SBPase activity decreases at 100 mM NaCl and above
NaF
-
0.01 M, 84% inhibition
oxidized glutathione
-
-
oxidized thioredoxin f
-
due to the formation of a stable complex between enzyme and thioredoxin
-
PCMB
-
0.2 mM, 35% inhibition
phosphate
-
competitive
Ribulose 1,5-diphosphate
-
inhibits at physiological concentrations
sedoheptulose-1,7-bisphosphate
-
competitive
sedoheptulose-1,7-bisphosphate
-
inhibits at physiological concentrations
glycerate
-
inhibits at physiological concentrations
additional information
-
no substrate inhibition up to 2 mM
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activates
Dithiol
-
absolute requirement for a dithiol at pH values below pH 7.7, i.e. reduced thioredoxin f or dithiothreitol
dithiothreitol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates; activation is strongly impaired by incubating oxidized enzyme in the presence of Fe2+ before addition of dithiothreitol
dithiothreitol
-
activation
NaCl
-
small increase of activity at 50 mM NaCl
reduced ferredoxin
-
required
reduced ferredoxin
-
activates in presence of Ca2+ or Mn2+
reduced ferredoxin
-
activates
reduced thioredoxin Fb
-
activates
-
Reducing agent
-
required
-
Reducing agent
-
required by native enzyme and recombinant enzyme
-
sedoheptulose 1,7-bisphosphate
-
activation
Thioredoxin f
-
activates
-
EDTA
-
increases activity
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.38
-
fructose 1,6-diphosphate
-
reduced enzyme
0.6
-
fructose 1,6-diphosphate
-
oxidized enzyme
0.013
-
sedoheptulose 1,7-bisphosphate
-
-
0.013
-
sedoheptulose 1,7-bisphosphate
-
without phosphate
0.013
-
sedoheptulose 1,7-bisphosphate
-
-
0.014
-
sedoheptulose 1,7-bisphosphate
-
at pH 8.2, in presence of 10 mM Mg2+
1
-
sedoheptulose 1,7-bisphosphate
-
at pH 6.0
0.0175
-
sedoheptulose 1,7-diphosphate
-
with 5 mM phosphate
0.0335
-
sedoheptulose 1,7-diphosphate
-
with 10 mM phosphate
0.05
-
sedoheptulose 1,7-diphosphate
-
reduced enzyme
0.42
-
sedoheptulose 1,7-diphosphate
-
oxidized enzyme
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.42
-
fructose 1,6-diphosphate
-
oxidized enzyme
21
-
fructose 1,6-diphosphate
-
reduced enzyme
0.84
-
sedoheptulose 1,7-diphosphate
-
oxidized enzyme
81
-
sedoheptulose 1,7-diphosphate
-
reduced enzyme
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.224
-
-
leaf enzyme extract
3.5
-
-
substrate fructose 1,6-bisphosphate, pH 8.3, 22°C
7.15
-
-
recombinant enzyme in the soluble fraction of Escherichia coli
28.6
-
-
-
additional information
-
-
-
additional information
-
-
enzyme activity in transgenic lines of Nicotiana tabacum
additional information
-
-
enzyme activity in wild-type plants and transgenic lines expressing the enzyme from Chlamydomonas sp. W80, photosynthetic activity in wild-type and transgenic plants, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.8
-
-
at 5 mM Mg2+
8.2
-
C4PAW8
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6
9.2
-
pH 7.6: about 45% of maximal activity, pH 9.2: about 75% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
C4PAW8
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.17
-
C4PAW8
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Cucumis sativus Jinyou 3
-
-
-
Manually annotated by BRENDA team
-
in mature, fully expanded leaves, enzyme activity of transgenic plants is closely related with photosynthetic capacity, in youngest leaves, photosynthetic rates are close to or higher than those of wild type plants
Manually annotated by BRENDA team
C4PAW8
high enzyme level, CsSBP expression at the mRNA and protein level is the highest in mid-position leaves, medium in base position leaves, and the lowest in upper position leaves. The SBPase activity decreases successively as leaf position declines
Manually annotated by BRENDA team
Cucumis sativus Jinyou 3
-
high enzyme level, CsSBP expression at the mRNA and protein level is the highest in mid-position leaves, medium in base position leaves, and the lowest in upper position leaves. The SBPase activity decreases successively as leaf position declines
-
Manually annotated by BRENDA team
Cucumis sativus Jinyou 3
-
-
-
Manually annotated by BRENDA team
additional information
-
expression profile of the enzyme in plant tissues, no activity and expression in roots
Manually annotated by BRENDA team
additional information
C4PAW8
no enzyme activity in roots, CsSBP expresses only in green tissues of cucumber plants, real-time quantitative RT-PCR enzyme expression analysis, overview
Manually annotated by BRENDA team
additional information
Cucumis sativus Jinyou 3
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no enzyme activity in roots, CsSBP expresses only in green tissues of cucumber plants, real-time quantitative RT-PCR enzyme expression analysis, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
exclusively located in chloroplast
Manually annotated by BRENDA team
-
chloroplast stroma contains at least two enzyme species capable of hydrolysing sedoheptulose-1,7-bisphosphate, EC 3.1.3.37 and the chloroplast fructose 1,6-bisphosphatase; stroma
Manually annotated by BRENDA team
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73-89% of total leaf SBPase is localized in the chloroplast
Manually annotated by BRENDA team
-
sedoheptulose bisphosphatase is located near thioredoxin m, but not near thioredoxin f, in chloroplast
Manually annotated by BRENDA team
-
determination of localization of and distance between enzymes involved in the fixation of CO2, overview
Manually annotated by BRENDA team
Cucumis sativus Jinyou 3
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
-
SDS-PAGE
56000
-
-
gel filtration
66000
-
-
gel filtration
75000
-
-
sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 38000, enzyme plus His6-tag plus transit peptide, x * 35000, mature enzyme, deduced from gene sequence
?
-
x * 41600, recombinant enzyme, SDS-PAGE
?
C4PAW8
x * 42000, about, sequence calculation
?
Cucumis sativus Jinyou 3
-
x * 42000, about, sequence calculation
-
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 38000, SDS-PAGE
tetramer
-
crystallization data
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
processing of 67 amino acids transit peptide
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dialysis for 16 h with only minor loss in activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
autooxidizable upon removal of reducing agents. The enzyme is activated when reduced by any of the thioredoxins
-
134830
upon transition from darkness to light, the enzyme shifts from an oxidized inactive form to a reduced active form
-
134846
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
-
134831
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, small loss of activity after several years
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged enzyme from Escherichia coli in one step by nickel affinity chelating chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Nicotiana tabacum chloroplasts
-
expression in Triticum aestivum and Arabidopsis thaliana: SBPase mRNA in Arabidopsis and Triticum is regulated in a light-dependent manner and is also influenced by the developmental stage of the leaf
-
overexpression in Nicotiana tabacum from a construct containing the CaMV 35S promoter and the nopaline synthase termination sequence
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expression in Nicotiana tabacum chloroplasts
-
functional overexpression as soluble His-tagged enzyme in Escherichia coli
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gene CsSBP, DNA and amino acid sequence determination and analysis, sequence comparisons
C4PAW8
fructose -1,6-/sedoheptulose-1,7-bisphosphatase, one enzyme with dual activity
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expressed in Oryza sativa japonica, cultivar zhonghua11
-
expressed in Oryza sativa plants zhonghua11
-
expressed in Nicotiana tabacum
-
expressed in Nicotiana tabacum chloroplasts
-
expression in Escherichia coli
-
gene sequence reveals homology with fructose 1,6-bisphosphatases
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in phytoplasma infected leaves
A8DUA7
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
construction of transgenic Nicotiana tabacum plants overexpressing the Arabidopsis thaliana enzyme in the chloroplasts, the transgenic plants show increased enzyme activity and increased photosynthetic CO2 fixation leading to increased dry weight, succinate and starch accumulation compared to the wild-type plants, phenotype overview
additional information
-
construction of transgenic Nicotiana tabacum plants overexpressing the Chlamydomonas enzyme in the chloroplasts, the transgenic plants show increased enzyme activity and increased photosynthetic CO2 fixation leading to increased dry weight, phenotype overview
additional information
-
antisense transgenic plants, in mature, fully expanded leaves, enzyme activity is closely related with photosynthetic capacity, in youngest leaves, photosynthetic rates are close to or higher than those of wild type plants, decreased enzymic activity also leads to reduction in carbohydrate levels, particularly in starch
additional information
-
construction of transgenic Nicotiana tabacum plants overexpressing the Chlamydomonas sp. W80 enzyme in the chloroplasts, the transgenic plants show increased enzyme activity and increased photosynthetic CO2 fixation leading to increased dry weight, phenotype overview
additional information
-
construction of transgenic Nicotiana tabacum plants overexpressing the Arabidopsis thaliana enzyme in the chloroplasts, the transgenic plants show increased enzyme activity and increased photosynthetic CO2 fixation leading to increased dry weight, succinate and starch accumulation compared to the wild-type plants, phenotype overview
additional information
-
a very low or virtually no activity of FBPase remains in the mutant DRHB1485
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
antisense transgenic plants, in mature, fully expanded leaves, enzyme activity is closely related with photosynthetic capacity, in youngest leaves, photosynthetic rates are close to or higher than those of wild type plants, decreased enzymic activity also leads to reduction in carbohydrate levels, particularly in starch
biotechnology
-
bifunctional fructose-1,6/seduheptulose-1,7-bisphosphatase expressed in Nicotiana tabacum, plants show enhanced photosynthetic efficiency and growth characteristics as well as higher photosynthetic CO2 fixation and more final dry matter