Information on EC 3.1.3.24 - sucrose-phosphate phosphatase

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

EC NUMBER
COMMENTARY hide
3.1.3.24
-
RECOMMENDED NAME
GeneOntology No.
sucrose-phosphate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sucrose 6F-phosphate + H2O = sucrose + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sucrose biosynthesis III
-
-
sucrose biosynthesis II
-
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sucrose biosynthesis I (from photosynthesis)
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Starch and sucrose metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
sucrose-6F-phosphate phosphohydrolase
Requires Mg2+ for maximal activity [2]. This is the final step in the sucrose-biosynthesis pathway. The enzyme is highly specific for sucrose 6-phosphate, with fructose 6-phosphate unable to act as a substrate [2]. Belongs in the haloacid dehydrogenase (HAD) superfamily. The F of sucrose 6F-phosphate is used to indicate that the fructose residue of sucrose carries the substituent.
CAS REGISTRY NUMBER
COMMENTARY hide
9059-33-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PCC 7120
SwissProt
Manually annotated by BRENDA team
Asclepias rotundifolia
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Bryum sp.
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Caturra, CCCA02 and CCCA12
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-
Manually annotated by BRENDA team
var. robusta FRT64 and FRT05
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
no activity in Agaricus campestris
-
-
-
Manually annotated by BRENDA team
no activity in Asparagopsis taxiformis
-
-
-
Manually annotated by BRENDA team
no activity in Cystophora subfarcinata
-
-
-
Manually annotated by BRENDA team
no activity in Ecklonia radiata
-
-
-
Manually annotated by BRENDA team
no activity in Hormosira banksii
-
-
-
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Saccharum spp.
-
-
-
Manually annotated by BRENDA team
gene sppA
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
sucrose-phosphate synthase, SPS, synthesizes sucrose-6F-phosphate from UDP-Glc and/or ADP-Glc and fructose-6-P, and it is metabolically associated to sucrose-phosphate phosphatase, SPP, a specific phosphatase, yielding the net synthesis of sucrose
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
2.5% of the activity with sucrose 6-phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
1.9% of the activity with sucrose 6-phosphate
-
-
?
fructose 1,6-diphosphate + H2O
?
show the reaction diagram
-
1.5% of the activity with sucrose 6-phosphate
-
-
?
p-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
-
5.0% of the activity with sucrose 6-phosphate
-
-
?
sucrose 6-phosphate + H2O
sucrose + phosphate
show the reaction diagram
sucrose phosphate + H2O
sucrose + phosphate
show the reaction diagram
-
-
-
?
UDP + H2O
?
show the reaction diagram
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1.7% of the activity with sucrose 6-phosphate
-
-
?
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
sucrose 6-phosphate + H2O
sucrose + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-nitrophenyl-alpha-L-galactopyranoside
-
-
6-kestose
Ammonium molybdate
AMP
-
68% residual activity at 5 mM
cellobiose
-
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D-Fructose 1-phosphate
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62% residual activity at 5 mM
D-glucose
-
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D-glucose 6-phosphate
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67% residual activity at 5 mM
D-ribose 5-phosphate
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9% residual activity at 5 mM
diphosphate
fluoride
5% inhibition at 2.5 mM
glucose
-
100 mM, 25% inhibition
maltose
melizitose
molybdate
12% inhibition at 2.5 mM
phosphate
Sucrose
trehalose
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-
turanose
vanadate
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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148% activity at 5 mM
D-fructose 1,6-bisphosphate
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124% activity at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.065 - 0.35
sucrose 6-phosphate
0.15
sucrose phosphate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
100
cellobiose
-
-
354
D-glucose
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100
maltose
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80 - 161
Sucrose
26
trehalose
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
4-nitrophenyl-alpha-L-galactopyranoside
Synechocystis sp.
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uncompetitive inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.37
recombinant enzyme in extract of expressing Escherichia coli
1.433
-
-
15.66
purified enzyme
1250
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
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6.4 - 6.7
Saccharum spp.
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
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pH 5.0: about 25% of maximal activity, pH 8.0: about 70% of maximal activity
5.5 - 8
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pH 5.5: about 50% of maximal activity, pH 8.0: about 65% of maximal activity
6 - 8
Saccharum spp.
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pH 6.0: about 20% of maximal activity, pH 8.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
germinating
Manually annotated by BRENDA team
Saccharum spp.
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-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Saccharum spp.
-
-
Manually annotated by BRENDA team
additional information
-
no activity detected in vacuole, chloroplast or mitochondria
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000 - 27000
native enzyme, gel filtration
28000
1 * 28000, native enzyme, SDS-PAGE, 1 * 28034, native enzyme, amino acid sequence calculation, 1 * 32000, recombinant His-tagged enzyme, SDS-PAGE
28034
1 * 28000, native enzyme, SDS-PAGE, 1 * 28034, native enzyme, amino acid sequence calculation, 1 * 32000, recombinant His-tagged enzyme, SDS-PAGE
32000
1 * 28000, native enzyme, SDS-PAGE, 1 * 28034, native enzyme, amino acid sequence calculation, 1 * 32000, recombinant His-tagged enzyme, SDS-PAGE
47213
x * 47213, DNA sequence calculation
50000
-
2 * 50000, SDS-PAGE
55000
-
2 * 55000, SDS-PAGE
84000
-
4 * 84000, SDS-PAGE
100000
-
gel filtration
115000
-
gel filtration
120000
-
gel filtration
336000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 47213, DNA sequence calculation
homotetramer
-
4 * 84000, SDS-PAGE
monomer
1 * 28000, native enzyme, SDS-PAGE, 1 * 28034, native enzyme, amino acid sequence calculation, 1 * 32000, recombinant His-tagged enzyme, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme alone and in complex with various ligands, protein consists of a core domain containing the catalytic site and a smaller cap domain that contains a glucose binding site
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
Saccharum spp.
-
20°C, 15 min, 97% loss of activity
114204
6
-
unstable below, bovine serum albumin reduces loss of activity
114200
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
Saccharum spp.
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pH 5.2, 15 min, 97% loss of activity
40
Saccharum spp.
-
10 min, complete loss of activity
100
Saccharum spp.
-
2 min, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, partially purified enzyme, 50% loss of activity after 7-8 days
-20°C, 10 mM HEPES buffer, pH 7, 50% glycerol, 1 mM dithiothreitol, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
25000fold, to homogeneity
-
partial
recombinant enzyme from Escherichia coli partially, and native for strain PCC 7120 3260fold
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)-pLysS by nickel affinity chromatography, ultrafiltration, anion exchange chromatography, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli DH5alpha as His-tagged enzyme
expression in Escherichia coli
gene sppA, genetic structure, expression analysis, heterologous expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)-pLysS
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
transgenic plants with reduced enzyme levels due to a RNA interference strategy, plants with less than 10% of wild-type activity display inhibition of photosynthesis, chlorosis, and reduced growth rates. They have strongly reduced levels of sucrose and hexoses but contain 3-5 times more starch than controls