BRENDA - Enzyme Database
show all sequences of 3.1.3.10

Glucose-1-phosphatase (AgpE) from Enterobacter cloacae displays enhanced phytase activity

Herter, T.; Berezina, O.V.; Zinin, N.V.; Velikodvorskaya, G.A.; Greiner, R.; Borriss, R.; Appl. Microbiol. Biotechnol. 70, 60-64 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Enterobacter cloacae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.31
-
D-glucose 1-phosphate
37C, pH 5.0
Enterobacter cloacae
0.47
-
D-glucose 6-phosphate
37C, pH 5.0
Enterobacter cloacae
0.51
-
myo-inositol hexakisphosphate
37C, pH 5.0
Enterobacter cloacae
0.62
-
D-Fructose 1-phosphate
37C, pH 5.0
Enterobacter cloacae
0.66
-
D-fructose 6-phosphate
37C, pH 5.0
Enterobacter cloacae
13
-
p-nitrophenyl phosphate
37C, pH 5.0
Enterobacter cloacae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
44000
-
2 * 44000, SDS-PAGE
Enterobacter cloacae
82500
-
gel filtration
Enterobacter cloacae
125000
-
PAGE
Enterobacter cloacae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Enterobacter cloacae
-
enzyme additionally can act as 3-phytase but is only able to cleave off the third phosphate group of myo-inositol
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
32
-
substrate myo-inositol hexakisphosphate, 37C, pH 5.0
Enterobacter cloacae
40
-
substrate D-fructose 6-phosphate, 37C, pH 5.0
Enterobacter cloacae
142
-
substrate D-fructose 1-phosphate, 37C, pH 5.0
Enterobacter cloacae
146
-
substrate D-glucose 1-phosphate, 37C, pH 5.0
Enterobacter cloacae
159
-
substrate D-glucose 6-phosphate, 37C, pH 5.0
Enterobacter cloacae
196
-
substrate D-glucose 1-phosphate, 37C, pH 5.0
Enterobacter cloacae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-fructose 1-phosphate + H2O
-
663741
Enterobacter cloacae
D-fructose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
-
663741
Enterobacter cloacae
D-fructose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
-
663741
Enterobacter cloacae
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
-
663741
Enterobacter cloacae
D-glucose + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
-
663741
Enterobacter cloacae
? + phosphate
enzyme is only able to cleave off the third phosphate group of myo-inositol
-
-
?
p-nitrophenyl phosphate + H2O
-
663741
Enterobacter cloacae
p-nitrophenol + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 44000, SDS-PAGE
Enterobacter cloacae
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
24
-
myo-inositol hexakisphosphate
37C, pH 5.0
Enterobacter cloacae
30
-
p-nitrophenyl phosphate
37C, pH 5.0
Enterobacter cloacae
105
-
D-fructose 6-phosphate
37C, pH 5.0
Enterobacter cloacae
109
-
D-glucose 6-phosphate
37C, pH 5.0
Enterobacter cloacae
111
-
D-Fructose 1-phosphate
37C, pH 5.0
Enterobacter cloacae
145
-
D-glucose 1-phosphate
37C, pH 5.0
Enterobacter cloacae
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Enterobacter cloacae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.31
-
D-glucose 1-phosphate
37C, pH 5.0
Enterobacter cloacae
0.47
-
D-glucose 6-phosphate
37C, pH 5.0
Enterobacter cloacae
0.51
-
myo-inositol hexakisphosphate
37C, pH 5.0
Enterobacter cloacae
0.62
-
D-Fructose 1-phosphate
37C, pH 5.0
Enterobacter cloacae
0.66
-
D-fructose 6-phosphate
37C, pH 5.0
Enterobacter cloacae
13
-
p-nitrophenyl phosphate
37C, pH 5.0
Enterobacter cloacae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
44000
-
2 * 44000, SDS-PAGE
Enterobacter cloacae
82500
-
gel filtration
Enterobacter cloacae
125000
-
PAGE
Enterobacter cloacae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
32
-
substrate myo-inositol hexakisphosphate, 37C, pH 5.0
Enterobacter cloacae
40
-
substrate D-fructose 6-phosphate, 37C, pH 5.0
Enterobacter cloacae
142
-
substrate D-fructose 1-phosphate, 37C, pH 5.0
Enterobacter cloacae
146
-
substrate D-glucose 1-phosphate, 37C, pH 5.0
Enterobacter cloacae
159
-
substrate D-glucose 6-phosphate, 37C, pH 5.0
Enterobacter cloacae
196
-
substrate D-glucose 1-phosphate, 37C, pH 5.0
Enterobacter cloacae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-fructose 1-phosphate + H2O
-
663741
Enterobacter cloacae
D-fructose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
-
663741
Enterobacter cloacae
D-fructose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
-
663741
Enterobacter cloacae
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
-
663741
Enterobacter cloacae
D-glucose + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
-
663741
Enterobacter cloacae
? + phosphate
enzyme is only able to cleave off the third phosphate group of myo-inositol
-
-
?
p-nitrophenyl phosphate + H2O
-
663741
Enterobacter cloacae
p-nitrophenol + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 44000, SDS-PAGE
Enterobacter cloacae
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
24
-
myo-inositol hexakisphosphate
37C, pH 5.0
Enterobacter cloacae
30
-
p-nitrophenyl phosphate
37C, pH 5.0
Enterobacter cloacae
105
-
D-fructose 6-phosphate
37C, pH 5.0
Enterobacter cloacae
109
-
D-glucose 6-phosphate
37C, pH 5.0
Enterobacter cloacae
111
-
D-Fructose 1-phosphate
37C, pH 5.0
Enterobacter cloacae
145
-
D-glucose 1-phosphate
37C, pH 5.0
Enterobacter cloacae
Other publictions for EC 3.1.3.10
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
749654
Suleimanova
Novel glucose-1-phosphatase w ...
Pantoea sp. 3.5.1
Appl. Environ. Microbiol.
81
6790-6799
2015
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1
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1
1
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2
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5
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1
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1
1
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5
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1
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1
1
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2
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1
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1
1
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5
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-
-
-
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1
1
-
-
-
715067
Kim
-
Gene cloning, expression, and ...
Enterobacter cloacae, Enterobacter cloacae B11
Fish. Aqua. Sci.
13
49-55
2010
-
-
1
-
-
-
1
-
1
2
1
4
-
2
-
-
1
-
-
-
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-
6
1
1
1
1
-
1
1
1
-
-
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-
1
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-
-
-
-
1
-
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1
2
1
4
-
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1
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-
6
1
1
1
1
-
1
1
1
-
-
-
-
-
-
-
704914
Kim
Purification, characterization ...
Citrobacter braakii
J. Gen. Appl. Microbiol.
55
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2009
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-
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4
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6
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1
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4
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1
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1
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1
1
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4
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2
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1
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-
4
-
1
-
1
-
1
1
-
-
-
-
-
-
-
-
691563
Greiner
-
Production of D-myo-inositol(1 ...
Pantoea agglomerans
Braz. Arch. Biol. Technol.
51
235-246
2008
-
-
1
-
-
1
-
2
-
-
-
1
-
1
-
-
1
-
-
-
1
-
3
-
2
1
1
2
1
1
1
-
-
-
-
-
-
1
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-
-
1
-
-
-
2
-
-
-
1
-
-
-
1
-
-
1
-
3
-
2
1
1
2
1
1
1
-
-
-
-
-
-
-
663741
Herter
Glucose-1-phosphatase (AgpE) f ...
Enterobacter cloacae
Appl. Microbiol. Biotechnol.
70
60-64
2006
-
-
1
-
-
-
-
6
-
-
3
-
-
3
-
-
-
-
-
-
6
-
6
1
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-
-
6
-
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1
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6
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3
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6
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6
1
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6
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-
652437
Lee
Functional insights revealed b ...
Escherichia coli
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31412-31418
2003
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1
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6
1
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2
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2
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-
-
-
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-
9
-
-
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6
3
3
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1
-
-
-
-
-
6
1
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-
2
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-
-
-
9
-
-
-
-
6
3
3
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-
-
-
-
-
-
-
649158
Jia
Purification, crystallization ...
Escherichia coli
Acta Crystallogr. Sect. D
57
314-316
2001
-
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1
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-
-
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2
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1
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5
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1
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1
1
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1
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2
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1
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1
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1
1
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134585
Joh
Isolation and properties of gl ...
Pholiota nameko
Biosci. Biotechnol. Biochem.
62
2251-2253
1998
-
-
-
-
-
-
5
9
-
3
1
6
-
2
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-
1
-
-
1
8
-
15
-
1
-
-
7
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
5
-
9
-
3
1
6
-
-
-
1
-
1
8
-
15
-
1
-
-
7
1
-
1
-
-
-
-
-
-
-
134583
Konichev
-
Metabolic role of the multiple ...
Bombyx mori
Biochemistry
62
543-550
1997
-
-
-
-
-
-
-
-
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6
3
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1
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1
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3
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7
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-
4
-
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-
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6
3
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-
-
1
-
3
-
-
7
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
134579
Pradel
Utilization of exogenous gluco ...
Escherichia coli
Res. Microbiol.
142
37- 45
1991
-
-
-
-
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6
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4
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1
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6
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6
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1
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6
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Dassa
The complete nucleotide sequen ...
Escherichia coli
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5497-5500
1990
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1
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Pradel
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Escherichia coli
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1
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134576
Pradel
Acid phosphatases of Escherich ...
Escherichia coli
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4916
1988
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1
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1
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13
1
1
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1
1
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1
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7
1
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1
6
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1
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13
1
1
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1
1
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Saugy
Phosphatases and phosphodieste ...
Pisum sativum
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5
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1
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2
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1
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1
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134584
Ching
Acid phosphatases and seed shr ...
Triticosecale Wittmack
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76
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3
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1
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1
1
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134580
Turner
The hydrolysis of glucose mono ...
Pisum sativum
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1960
-
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5
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1
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1
11
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1
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2
1
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1
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5
1
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2
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1
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2
1
11
-
1
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2
1
-
-
-
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-
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-
134582
Faulkner
A hexose-1-phosphatase in silk ...
Bombyx mori
Biochem. J.
60
590-596
1955
-
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-
-
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4
-
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2
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2
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1
16
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1
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1
1
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4
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5
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1
16
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1
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1
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