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
3.1.3.10
-
RECOMMENDED NAME
GeneOntology No.
glucose-1-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
glucose and glucose-1-phosphate degradation
-
Glycolysis / Gluconeogenesis
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose-1-phosphate phosphohydrolase
Also acts, more slowly, on D-galactose 1-phosphate.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acid glucose-1-phosphatase
-
-
acid glucose-1-phosphatase
Enterobacter cloacae B11
-
-
-
acid glucose-1-phosphatase
-
-
acid phosphatase
-
acid phosphatase is unequal to glucose-1-phosphatase
acid phosphatase
-
-
acid phosphatase
-
-
AGP
Enterobacter cloacae B11
-
-
-
agpC
D3GGN3
-
G-1-Pase
Triticosecale Wittmack
-
-
G1Pase
-
-
-
-
glucose monophosphatase
-
-
glucose-1-phosphate-phosphatase
-
-
hexose-1-phosphatase
-
-
pea-seed acid phosphatase
-
-
periplasmic acid glucose-1-phosphatase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-38-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
L.var. white, yellow, zebra
-
-
Manually annotated by BRENDA team
enzyme additionally can act as 3-phytase but is only able to cleave off the third phosphate group of myo-inositol
-
-
Manually annotated by BRENDA team
isolate from seawater, gene AgpEnB11
-
-
Manually annotated by BRENDA team
Enterobacter cloacae B11
isolate from seawater, gene AgpEnB11
-
-
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phosphoglycerate + H2O
2,3-dihydroxypropanoic acid + phosphate
show the reaction diagram
-
-
-
?
3-phosphoglycerate + H2O
2,3-dihydroxypropanoic acid + phosphate
show the reaction diagram
-
hydrolysis is more rapid than that of glucose monophosphates
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
hydrolysis is more rapid than that of glucose monophosphate
-
?
ADP + H2O
AMP + 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
Enterobacter cloacae, Enterobacter cloacae B11
-
high activity
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae B11
-
high activity
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
enzyme form GP3 of the fat body is inactive with AMP
-
-
-
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Triticosecale Wittmack
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
enzyme forms GP3 and GP3'
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
hydrolysis more rapid than that of glucose monophosphates
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
r
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
hydrolysis was more rapid than that of glucose monophosphates
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
-, ?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
r
D-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
?
D-fructose 1-phosphate + 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-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
r
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-, D3GGN3
-
-
-
?
D-galactose 1-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
-
-
-
r
D-galactose 1-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
-
-
-
-
-
D-galactose 1-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
-
-
-
?
D-galactose 1-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
-
-
-
-
ir
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 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
-
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
r
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
ir
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Triticosecale Wittmack
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Q1W5Y8
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-, D3GGN3
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
multiple forms of glucose-1-phosphatase specify for glucose 1-phosphate and galactose 1-phosphate in hemolymph of the silkworm
-
-
ir
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Q1W5Y8
activity of recombinant enzyme towards glucose 1-phosphate shown to be 4.8fold higher than activity towards myo-inositol hexakisphosphate (phytate), kinetic parameters affected by entrapment of the enzyme in alginate beads
-
-
?
D-glucose 6-phosphate
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-, ?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
-
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-, D3GGN3
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
no catalysis
-
-
-
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
the enzyme acts as a D-glucose scavenger
-
?
D-mannose 6-phosphate + H2O
D-mannose + phosphate
show the reaction diagram
-, D3GGN3
-
-
-
?
D-ribose 5-phosphate
D-ribose + phosphate
show the reaction diagram
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
-
-
-
?
D-ribose 5-phosphate + H2O
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 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol hexakisphosphate + H2O
?
show the reaction diagram
-
-
-
?
myo-inositol hexakisphosphate + H2O
?
show the reaction diagram
-
-
enzyme is only able to cleave off the third phosphate group of myo-inositol
-
?
myo-inositol hexakisphosphate + H2O
?
show the reaction diagram
-
the enzyme is potentially involved in pathogenic inositol phosphate signal transduction pathways via type III secretioin into the host cell
-
?
myo-inositol hexakisphosphate + H2O
D-myo-inositol(1,2,4,5,6)pentakisphosphate + phosphate
show the reaction diagram
Q1W5Y8
i.e. phytate, kinetic parameters affected by entrapment of the enzyme in alginate beads, conversion into one single myo-inositol pentakisphosphate isomer
-
-
?
p-nitrophenyl phosphate
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
-
-
-
?
glycerol 3-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
Enterobacter cloacae, Enterobacter cloacae B11
-
the enzyme hydrolyzes a wide variety of phosphorylated compounds, primarily small monosaccharide phosphates, overview
-
-
-
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
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae B11
-
high activity
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Enterobacter cloacae, Enterobacter cloacae B11
-
high activity
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
-
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
r
D-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
-
D-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
r
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-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
r
D-fructose 6-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
-
-
-
r
D-galactose 1-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
-
-
-
-
-
D-galactose 1-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
-
-
-
-
ir
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 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
r
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
ir
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Triticosecale Wittmack
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Q1W5Y8
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
multiple forms of glucose-1-phosphatase specify for glucose 1-phosphate and galactose 1-phosphate in hemolymph of the silkworm
-
-
ir
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
-
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
the enzyme acts as a D-glucose scavenger
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol hexakisphosphate + H2O
?
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 ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)6Mo7O24
-
98% inhibition of 4 -nitrophenyl phosphate hydrolysis by 1.0 mM
ATP
-
18.5% inhibition of D-glucose 1-phosphate hydrolysis by 1.0 mM
CuSO4
-
55% inhibition of 4-nitrophenyl phosphate hydrolysis by 10 mM
GDP
-
31% inhibition of D-glucose 1-phosphate hydrolysis by 1.0 mM
GTP
-
23.7% inhibition of D-glucose 1-phosphate hydrolysis by 1.0 mM
HgCl2
-
74% inhibition of D-glucose 1-phosphate hydrolysis by 0.2 mM
HgCl2
-
99% inhibition of 4-nitrophenyl phosphate hydrolysis by 10 mM
iodoacetic acid
-
69% inhibition of D-glucose 1-phosphate hydrolysis by 10 mM
Na2MoO4
-
100% inhibition of D-glucose 1-phosphate hydrolysis by 1.0 mM
Na2MoO4
-
50% inhibition of membrane bound activity by 0.1 mM
Na3As04
-
85% inhibition of D-glucose 1-phosphate hydrolysis by 10 mM
Na3VO4
-
50% inhibition of membrane bound activity by 0.1 mM
NaF
-
75% inhibition of D-glucose 1-phosphate hydrolysis by 2.0 mM, 100% inhibition of D-glucose 1-phosphate hydrolysis by 20 mM
NaF
-
56% inhibition of D-glucose 1-phosphate hydrolysis by 0.2 mM
NaF
-
no inhibition through NaF for the acid phosphatase AP35
phosphate
-
36% inhibition of D-glucose 1-phoshate hydrolysis by 0.075 mM, 52% inhibition of D-glucose 1-phosphate hydrolysis by 0.15 mM
phosphate
-
54% inhibition of D-glucose 1-phosphate hydrolysis by 10 mM
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.2
-
4-nitrophenyl phosphate
-
-
30
-
4-nitrophenyl phosphate
-
-
13.4
-
Adenosine diphosphate
-
-
56.7
-
Adenosine triphosphate
-
-
0.62
-
D-Fructose 1-phosphate
-
37C, pH 5.0
2.2
-
D-Fructose 1-phosphate
-
-
12.2
-
D-Fructose 1-phosphate
-
-
50
-
D-Fructose 1-phosphate
-
-
0.66
-
D-fructose 6-phosphate
-
37C, pH 5.0
14.3
-
D-fructose 6-phosphate
-
-
25
-
D-fructose 6-phosphate
-
-
85.4
-
D-galactose 1-phosphate
-
-
0.31
-
D-glucose 1-phosphate
-
37C, pH 5.0
0.39
-
D-glucose 1-phosphate
-
pH 6.5
0.5
-
D-glucose 1-phosphate
-
-
4.8
-
D-glucose 1-phosphate
-
-
5.12
-
D-glucose 1-phosphate
-, D3GGN3
Vmax: 1.9 micromol/min/mg
0.47
-
D-glucose 6-phosphate
-
37C, pH 5.0
0.5
-
D-glucose 6-phosphate
-, D3GGN3
Vmax: 0.8 micromol/min/mg
1.6
-
D-glucose 6-phosphate
-
-
1.9
-
D-glucose 6-phosphate
-, D3GGN3
Vmax: 2.2 micromol/min/mg
15
-
D-glucose 6-phosphate
-
-
9
-
D-mannose 6-phosphate
-, D3GGN3
Vmax: 2.6 micromol/min/mg
7.9
-
D-ribose 5-phosphate
-
-
11
-
D-ribose 5-phosphate
-
-
30
-
D-ribose 5-phosphate
-
-
100
-
Glycerol 2-phosphate
-
-
0.35
-
myo-inositol hexakisphosphate
Q1W5Y8
free enzyme, pH 4.5, 37C
0.51
-
myo-inositol hexakisphosphate
-
37C, pH 5.0
0.54
-
myo-inositol hexakisphosphate
-
pH 4.5
0.84
-
myo-inositol hexakisphosphate
Q1W5Y8
entrapped enzyme, pH 4.5, 37C
13
-
p-nitrophenyl phosphate
-
pH 3.5
13
-
p-nitrophenyl phosphate
-
37C, pH 5.0
12.3
-
phosphoenolpyruvate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0035
-
ADP
-
-
95
-
D-Fructose 1-phosphate
-
-
111
-
D-Fructose 1-phosphate
-
37C, pH 5.0
105
-
D-fructose 6-phosphate
-
37C, pH 5.0
117
-
D-glucose 1-phosphate
-
pH 6.5
145
-
D-glucose 1-phosphate
-
37C, pH 5.0
82
-
D-glucose 6-phosphate
-
-
109
-
D-glucose 6-phosphate
-
37C, pH 5.0
42
-
D-ribose 5-phosphate
-
-
0.00217
-
fructose 1-phosphate
-
-
0.00167
-
fructose 6-phosphate
-
-
0.0348
-
Galactose 1-phosphate
-
-
0.0393
-
glucose 1-phosphate
-
-
8
-
myo-inositol hexakisphosphate
Q1W5Y8
entrapped enzyme, pH 4.5, dropped as a consequence of entrapment
12
-
myo-inositol hexakisphosphate
-
pH 4.5
20.5
-
myo-inositol hexakisphosphate
Q1W5Y8
free enzyme, pH 4.5
24
-
myo-inositol hexakisphosphate
-
37C, pH 5.0
3
6
p-nitrophenyl phosphate
-
pH 3.5
30
-
p-nitrophenyl phosphate
-
37C, pH 5.0
0.000667
-
phosphoenolpyruvate
-
-
0.0005
-
ribose 5-phosphate
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
Na2MoO4
-
-
0.1
-
Na2MoO4
-
membrane bound activity
0.1
-
Na3VO4
-
membrane bound activity
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
with nitrophenyl phosphate as substrate, purification procedure described; with ribose 5-phosphate as substrate, purification procedure described
32
-
-
substrate myo-inositol hexakisphosphate, 37C, pH 5.0
40
-
-
purification procedure described; with phosphoenolpyruvate as substrate
40
-
-
substrate D-fructose 6-phosphate, 37C, pH 5.0
100
-
-
purification procedure described; with D-glucose 1-phosphate as substrate
100
-
-
with D-fructose 6-phosphate as substrate, purification procedure described
130
-
-
purification procedure described; with D-fructose 1-phosphate as substrate
142
-
-
substrate D-fructose 1-phosphate, 37C, pH 5.0
146
-
-
substrate D-glucose 1-phosphate, 37C, pH 5.0
159
-
-
substrate D-glucose 6-phosphate, 37C, pH 5.0
196
-
-
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
-
Q1W5Y8
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
-
-
p-nitrophenyl phosphate as substrate
4
4.5
-
-
4
5
-
with 4-nitrophenyl phosphate 25 mM as substrate
4
-
-
enzyme form GP3'
4.5
-
-
myo-inositol hexakisphophate as substrate
4.5
-
Q1W5Y8
determined for the free and the entrapped enzyme
4.8
-
-
enzyme forms GP1, GP2 and GP5
5
-
Triticosecale Wittmack
-
-
5
-
-, D3GGN3
assay at and optimal pH
5
-
-
recombinant His-tagged enzyme
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
7.5
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
8
Q1W5Y8
phytate dephosphorylation by the alginate reactor analyzed
3
9
-
with 4-nitrophenyl-phosphate 25 mM as substrate
3.5
7.5
-, D3GGN3
-
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
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
temperature used in the assay with D-glucose 1-phosphate in 0.75mM Tris-acetic acid-buffer, pH5.4
30
-
-
temperature used in the assay with 4-nitrophenyl phosphate in 50 mM Tris-HCl buffer, pH 7.5
30
-
-
temperature used in the assay with D-glucose 1-phosphate between 0.5 and 4 mM
30
-
Triticosecale Wittmack
-
-
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
-
-, D3GGN3
assay at and optimal temperature
50
-
-
recombinant His-tagged enzyme
60
-
Q1W5Y8
free enzyme exhibits maximal activity at
70
-
Q1W5Y8
maximum catalytic activity of entrapped enzyme at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
80
Q1W5Y8
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 ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Triticosecale Wittmack
-
-
Manually annotated by BRENDA team
-
enzyme forms GP2 and GP3
Manually annotated by BRENDA team
-
enzyme forms GP1, GP4, GP5
Manually annotated by BRENDA team
-
enzyme form GP3'
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Enterobacter cloacae B11
-
-
-
Manually annotated by BRENDA team
-
periplasm extracts made by osmotic shock of strain SBS1405(pEP1376)
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35000
-
-
enzyme form GP1 present in hemolymph
35000
-
-
SDS-PAGE
43710
-
-, D3GGN3
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
-
-
calculalted from amino acid sequence
46000
-
-, D3GGN3
SDS-PAGE
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
125000
-
-
PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 47000, recombinant His-tagged enzyme, SDS-PAGE
?
Enterobacter cloacae B11
-
x * 47000, recombinant His-tagged enzyme, SDS-PAGE
-
dimer
-
1 * 44000 + 1 * 44000, SDS-PAGE
dimer
-
two monomers of enzyme in asymmetric unit
dimer
-
2 * 44000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
X-ray analysis
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
10
-
stability profile, overview
3
7
-
purified enzyme, with 4-nitrophenyl phosphate 15 mM as substrate, activity rapidly lost above pH8
additional information
-
Q1W5Y8
pH dependence not affected by entrapment in alginate beads
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
70
-
stability profile, overview
55
-
-, D3GGN3
enzyme ist stable up to 55C 30 min
additional information
-
Q1W5Y8
temperature stability enhanced as a consequence of entrapment in alginate beads
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
entrapped enzyme shows a high operational stability by retaining almost full activity even after ten uses
Q1W5Y8
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-28 C,blood, at least 3 months without loss of activity
-
-15 C, water, 2 months, little loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
multiple enzyme forms GP1-GP5
-
(NH4)2SO4 precipitation, DEAE-sepharose chromatography, CM-sepharose chromatography and FPLC chromatography
-, D3GGN3
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
gel filtration
Q1W5Y8
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene AgpEnB11, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
in vivo cloning technique with plasmid Mu dII4042, expression in Escherichia coli strain SBS1295
-
plasmid cloning with pEP1376, a derivate of pBR322 carrying a 1,8-kb DNA fragment containing the entire agp gene
-
expressed in Escherichia coli BL21(DE3), pET-22b(+) and pIP5 vectors
Q1W5Y8