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 hide
3.1.3.37
-
RECOMMENDED NAME
GeneOntology No.
sedoheptulose-bisphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Calvin-Benson-Bassham cycle
-
-
Carbon fixation in photosynthetic organisms
-
-
Metabolic pathways
-
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Microbial metabolism in diverse environments
-
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photosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-1,7-bisphosphate 1-phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9055-32-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
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
strain H16
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain PCC7942
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-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
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
5.5% 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
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activation
Mn2+
-
can partially replace Mg2+ in activation
additional information
-
no requirement for divalent cation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxy-N'-((6-methyl-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
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-
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2-methyl-N'-((6-methyl-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
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-
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2-[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]-N'-[(E)-(4-methylphenyl)methylidene]acetohydrazide
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2-[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]-N'-[(E)-(5-hydroxy-2-methylphenyl)methylidene]acetohydrazide
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-
2-[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]-N-(2,3-dihydro-1H-inden-5-yl)acetamide
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-
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'-((4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
-
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3-bromo-N'-((6-(tert-butyl)-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
-
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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
-
-
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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
-
-
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3-bromo-N'-((6-isopropyl-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
-
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3-bromo-N'-((6-methyl-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
-
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3-bromo-N'-((6-nitro-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
-
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3-hydroxy-N'-((4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
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-
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3-methyl-N'-((4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
-
-
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3-nitro-N'-((4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
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4-bromo-N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
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-
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4-[1-(4-chlorobenzyl)-1H-indol-2-yl]-1,2,5-oxadiazol-3-amine
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acrolein
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treatment of intact chloroplast
Cu2+
-
0.1 mM, 30% inhibition
dehydroascorbate
-
-
fructose 1,6-diphosphate
-
at high concentrations
glycerate
-
inhibits at physiological concentrations
methyl 4-([[2-(4-amino-1,2,5-oxadiazol-3-yl)-1H-indol-1-yl]acetyl]amino)benzoate
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N'-((4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
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N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)-4-(trifluoromethyl)benzohydrazide
-
-
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N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)-4-fluorobenzohydrazide
-
-
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N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)-4-hydroxybenzohydrazide
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N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)-4-methylbenzohydrazide
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N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)-4-nitrobenzohydrazide
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N'-((6-bromo-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
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N'-((6-methyl-4-oxo-4H-chromen-3-yl)methylene)benzohydrazide
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NaCl
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SBPase activity decreases at 100 mM NaCl and above
NaF
-
0.01 M, 84% inhibition
oxidized glutathione
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-
oxidized thioredoxin f
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due to the formation of a stable complex between enzyme and thioredoxin
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PCMB
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0.2 mM, 35% inhibition
phosphate
Ribulose 1,5-diphosphate
-
inhibits at physiological concentrations
sedoheptulose-1,7-bisphosphate
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
EDTA
-
increases activity
NaCl
-
small increase of activity at 50 mM NaCl
reduced ferredoxin
reduced thioredoxin Fb
-
activates
-
Reducing agent
sedoheptulose 1,7-bisphosphate
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activation
Thioredoxin f
-
activates
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38 - 0.6
fructose 1,6-diphosphate
0.013 - 1
sedoheptulose 1,7-bisphosphate
0.0175 - 0.42
sedoheptulose 1,7-diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.42 - 21
fructose 1,6-diphosphate
4.2
sedoheptulose 1,7-bisphosphate
Synechocystis sp.
-
in 50 mM Tris/HCl, pH 8.0, 15 mM MgCl2, 10 mM dithiothreitol, at 289C
0.84 - 81
sedoheptulose 1,7-diphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.5
sedoheptulose 1,7-bisphosphate
Synechocystis sp.
-
in 50 mM Tris/HCl, pH 8.0, 15 mM MgCl2, 10 mM dithiothreitol, at 289C
4281
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
Ca2+
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.224
-
leaf enzyme extract
3.5
-
substrate fructose 1,6-bisphosphate, pH 8.3, 22C
7.15
-
recombinant enzyme in the soluble fraction of Escherichia coli
28.6
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
at 5 mM Mg2+
8.2 - 8.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6 - 9.2
-
pH 7.6: about 45% of maximal activity, pH 9.2: about 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.17
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
SDS-PAGE
56000
-
gel filtration
66000
-
gel filtration
75000
-
sucrose density gradient centrifugation
132000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
-
4 * 33000, SDS-PAGE
tetramer
-
crystallization data
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
processing of 67 amino acids transit peptide
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 100 mM HEPES, pH 7.5, 1.6 M ammonium sulfate, 7-9% (v/v) glycerol
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis for 16 h with only minor loss in activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
autooxidizable upon removal of reducing agents. The enzyme is activated when reduced by any of the thioredoxins
-
134830
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
upon transition from darkness to light, the enzyme shifts from an oxidized inactive form to a reduced active form
-
134846
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, small loss of activity after several years
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+-NTA resin column chromatography
-
recombinant His-tagged enzyme from Escherichia coli in one step by nickel affinity chelating chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Corynebacterium glutamicum and Escherichia coli BL21(DE3) cells
-
expressed in Dunaliella bardawil strain ATCC 30861
expressed in Escherichia coli BL21(DE3) cells
expressed in Nicotiana tabacum
-
expressed in Nicotiana tabacum chloroplasts
-
expressed in Oryza sativa japonica, cultivar zhonghua11
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expressed in Oryza sativa plants zhonghua11
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expression in Escherichia coli
-
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
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fructose -1,6-/sedoheptulose-1,7-bisphosphatase, one enzyme with dual activity
-
functional overexpression as soluble His-tagged enzyme in Escherichia coli
-
gene CsSBP, DNA and amino acid sequence determination and analysis, sequence comparisons
gene sequence reveals homology with fructose 1,6-bisphosphatases
-
overexpression in Nicotiana tabacum from a construct containing the CaMV 35S promoter and the nopaline synthase termination sequence
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in phytoplasma infected leaves
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D198A
-
inactive
D200A
-
inactive
D33A
-
inactive
D97A
-
inactive
E100A
-
inactive
E225A
-
inactive
E57A
-
inactive
K134A
-
inactive
K29A
-
the mutant shows increased activity compared to the wild type enzyme
R176A
-
inactive
R178G
-
the mutant shows very low activity compared to the wild type enzyme
T102A
-
inactive
Y131A
-
inactive
D198A
-
inactive
-
D97A
-
inactive
-
E57A
-
inactive
-
R176A
-
inactive
-
Y131A
-
inactive
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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