Information on EC 3.1.3.10 - glucose-1-phosphatase

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

EC NUMBER
COMMENTARY hide
3.1.3.10
-
RECOMMENDED NAME
GeneOntology No.
glucose-1-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glucose and glucose-1-phosphate degradation
-
-
Glycolysis / Gluconeogenesis
-
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Microbial metabolism in diverse environments
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-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose-1-phosphate phosphohydrolase
Also acts, more slowly, on D-galactose 1-phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-38-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
isolate from seawater, gene AgpEnB11
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
L.var. 99L, var.Alaska
-
-
Manually annotated by BRENDA team
Triticosecale Wittmack
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phosphoglycerate + H2O
2,3-dihydroxypropanoic acid + phosphate
show the reaction diagram
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
ADP + H2O
AMP + phosphate
show the reaction diagram
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
AMP + H2O
adenosine + phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
show the reaction diagram
D-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
D-galactose 1-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
D-glucose 6-phosphate
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
D-mannose 6-phosphate + H2O
D-mannose + phosphate
show the reaction diagram
-
-
-
?
D-ribose 5-phosphate
D-ribose + phosphate
show the reaction diagram
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
fructose 1-phosphate
fructose + phosphate
show the reaction diagram
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
glycerol 3-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
show the reaction diagram
myo-inositol hexakisphosphate + H2O
D-myo-inositol(1,2,4,5,6)pentakisphosphate + phosphate
show the reaction diagram
i.e. phytate, kinetic parameters affected by entrapment of the enzyme in alginate beads, conversion into one single myo-inositol pentakisphosphate isomer
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-
?
p-nitrophenyl phosphate
p-nitrophenol + phosphate
show the reaction diagram
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-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
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-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + 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
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
show the reaction diagram
D-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
D-galactose 1-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
myo-inositol hexakisphosphate + H2O
? + phosphate
show the reaction diagram
-
the enzyme is potentially involved in pathogenic inositol phosphate signal transduction pathways via type III secretioin into the host cell
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates
CaCl2
-
relative activity in presence of CaCl2 10mM 123%
Co2+
-
activates
EDTA
-
relative activity in presence of EDTA 10mM 104%
NaF
-
relative activity in presence of NaF 10mM 114%
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)6Mo7O24
-
98% inhibition of 4 -nitrophenyl phosphate hydrolysis by 1.0 mM
ATP
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18.5% inhibition of D-glucose 1-phosphate hydrolysis by 1.0 mM
CuSO4
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55% inhibition of 4-nitrophenyl phosphate hydrolysis by 10 mM
GDP
-
31% inhibition of D-glucose 1-phosphate hydrolysis by 1.0 mM
GTP
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23.7% inhibition of D-glucose 1-phosphate hydrolysis by 1.0 mM
iodoacetic acid
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69% inhibition of D-glucose 1-phosphate hydrolysis by 10 mM
Na2MoO4
Na3As04
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85% inhibition of D-glucose 1-phosphate hydrolysis by 10 mM
Na3VO4
-
50% inhibition of membrane bound activity by 0.1 mM
phosphate
Sodium citrate
-
25% inhibition of D-glucose 1-phosphate hydrolysis by 10 mM
tartaric acid
-
36% inhibition of 4-nitrophenyl phosphate hydrolysis by 10 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 30
4-nitrophenyl phosphate
13.4
Adenosine diphosphate
-
-
56.7
Adenosine triphosphate
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-
0.62 - 50
D-Fructose 1-phosphate
0.66 - 25
D-fructose 6-phosphate
85.4
D-galactose 1-phosphate
-
-
0.31 - 5.12
D-glucose 1-phosphate
0.47 - 15
D-glucose 6-phosphate
9
D-mannose 6-phosphate
Vmax: 2.6 micromol/min/mg
7.9 - 30
D-ribose 5-phosphate
100
Glycerol 2-phosphate
-
-
0.35 - 0.84
myo-inositol hexakisphosphate
13
p-nitrophenyl phosphate
12.3
phosphoenolpyruvate
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0035
ADP
Pholiota nameko
-
-
95 - 111
D-Fructose 1-phosphate
105
D-fructose 6-phosphate
Enterobacter cloacae
-
37C, pH 5.0
117 - 145
D-glucose 1-phosphate
82 - 109
D-glucose 6-phosphate
42
D-ribose 5-phosphate
Escherichia coli
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-
0.00217
fructose 1-phosphate
Pholiota nameko
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-
0.00167
fructose 6-phosphate
Pholiota nameko
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-
0.0348
Galactose 1-phosphate
Pholiota nameko
-
-
0.0393
glucose 1-phosphate
Pholiota nameko
-
-
8 - 24
myo-inositol hexakisphosphate
3 - 30
p-nitrophenyl phosphate
0.000667
phosphoenolpyruvate
Pholiota nameko
-
-
0.0005
ribose 5-phosphate
Pholiota nameko
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
Na2MoO4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
with nitrophenyl phosphate as substrate, purification procedure described; with ribose 5-phosphate as substrate, purification procedure described
32
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substrate myo-inositol hexakisphosphate, 37C, pH 5.0
130
-
purification procedure described; with D-fructose 1-phosphate as substrate
142
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substrate D-fructose 1-phosphate, 37C, pH 5.0
146
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substrate D-glucose 1-phosphate, 37C, pH 5.0
159
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substrate D-glucose 6-phosphate, 37C, pH 5.0
196
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substrate D-glucose 1-phosphate, 37C, pH 5.0
210
-
purification procedure described; with adenosine diphosphate as substrate
410
-
purification procedure described; with adenosine triphosphate as substrate
637
-
purification procedure described; with D-glucose 6-phosphate as substrate
2090
-
purification procedure described; with D-galactose 1-phosphate as substrate
2360
-
purification procedure described; with D-glucose 1-phosphate as substrate
additional information
specific activities of recombinant enzymes similar to those of wild-type towards myo-inositol hexakisphosphate (i.e. phytate) and glucose 1-phosphate as substrates, entrapment in alginate beads, free enzyme looses less than 5% phosphatase activity within 2 h in 20 mM Tris-HCl buffer, pH 8.0, transfer limitation is responsible for the reduced reaction rate of the entrapped enzyme, complete conversion of myo-inositol hexakisphosphate into one single myo-inositol pentakisphosphate isomer, identified as D-myo-inositol(1,2,4,5,6)pentakisphosphate, shown to be feasible by using the enzyme-loaded alginate beads in batch operations
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
p-nitrophenyl phosphate as substrate
4 - 4.5
-
-
4
-
enzyme form GP3'
4 - 5
-
with 4-nitrophenyl phosphate 25 mM as substrate
4.8
-
enzyme forms GP1, GP2 and GP5
5.2
-
enzyme form GP4
5.4
-
with 0.5 mM D-glucose 6-phosphate as substrate
5.5 - 5.7
-
with 0,5 mM D-glucose 1-phosphate as substrate
5.6
-
enzyme form GP3
5.9
-
purified enzyme; with 4-nitrophenyl phosphate 15 mM, as substrate
6.5
-
D-glucose 1-phosphate as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 10
-
activity profile, overview
2.5 - 7.5
-
about 50% of maximal activity at pH 6.5 with 10 mM D-glucose 1-phosphate
2.5 - 9.5
-
D-glucose 1-phosphate as substrate
3 - 6.5
-
p-nitrophenyl phosphate as substrate
3 - 7
-
myo-inositol hexakisphophate as substrate
3 - 9
-
with 4-nitrophenyl-phosphate 25 mM as substrate
3 - 8
phytate dephosphorylation by the alginate reactor analyzed
4 - 7.5
-
about 40% of maximal activity at pH 6.6 with 0.5 mM D-glucose 1-phosphate or with 0.5 mM D-glucose 6-phosphate
5 - 5.5
Triticosecale Wittmack
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
temperature used in the assay with 25 mM 4-nitrophenyl phosphate in 50 mM potassium phthalate-HCl buffer pH 4.5
40
-
with 4-nitrophenyl phosphate as substrate
45
assay at and optimal temperature
50
-
recombinant His-tagged enzyme
60
free enzyme exhibits maximal activity at
70
maximum catalytic activity of entrapped enzyme at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 80
activities of free and entrapped enzyme determined at, dephosphorylation of myo-inositol hexakisphosphate (phytate) increases with raising temperature, compared to the free-form activity, reaction rate of the alginate reactor is markedly reduced, 30-75% depending on temperature
30 - 70
-
activity profile, overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
Triticosecale Wittmack
-
-
Manually annotated by BRENDA team
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membrane
Manually annotated by BRENDA team
-
enzyme forms GP2 and GP3
Manually annotated by BRENDA team
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enzyme forms GP1, GP4, GP5
Manually annotated by BRENDA team
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enzyme form GP3'
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43710
calculated from cDNA
44000
-
SDS-Page of osmotic shock fluid of strain SBS1405(pEP1376)
45000
-
enzyme form GP2 present in the fat body; gel filtration Sephadex G-75, G100, ion-exchange chromatography on ADP-Sepharose, preparative isoelectrofocusing with Ampholines, preparative electrophoresis in blocks of polyacrylamide gel
45680
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calculalted from amino acid sequence
52000
-
enzyme form GP4 present in hemolymph
54000
-
enzyme form GP3' present in the fat body
55000
-
enzyme form GP3 present in the fat body; multiple forms of certain enzyms were isolated using a combination of the methods above
82500
-
gel filtration
102000
-
enzyme form GP5 present in hemolymph
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
determination of crystal structure by multiwavelength anomalous dispersion using a tungstate derivate together with the H18A inactive mutant complex structure with D-glucose 1-phosphate at 2.4 A resolution
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X-ray analysis
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 10
-
stability profile, overview
715067
3 - 7
-
purified enzyme, with 4-nitrophenyl phosphate 15 mM as substrate, activity rapidly lost above pH8
134585
additional information
pH dependence not affected by entrapment in alginate beads
691563
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
-
stability profile, overview
55
enzyme ist stable up to 55C 30 min
additional information
temperature stability enhanced as a consequence of entrapment in alginate beads
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
entrapped enzyme shows a high operational stability by retaining almost full activity even after ten uses
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15 C, water, 2 months, little loss of activity
-
-28 C,blood, at least 3 months without loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(NH4)2SO4 precipitation, DEAE-sepharose chromatography, CM-sepharose chromatography and FPLC chromatography
multiple enzyme forms GP1-GP5
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3), pET-22b(+) and pIP5 vectors
gene AgpEnB11, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
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in vivo cloning technique with plasmid Mu dII4042, expression in Escherichia coli strain SBS1295
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plasmid cloning with pEP1376, a derivate of pBR322 carrying a 1,8-kb DNA fragment containing the entire agp gene
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Show AA Sequence (362 entries)
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