BRENDA - Enzyme Database
show all sequences of 3.1.3.10

Purification, characterization, and gene cloning of glucose-1-phosphatase from Citrobacter braakii

Kim, Y.O.; Kim, H.W.; Park, I.S.; Lee, J.H.; Lee, S.J.; Kim, K.K.; J. Gen. Appl. Microbiol. 55, 345-350 (2009)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.5
-
D-glucose 6-phosphate
Vmax: 0.8 micromol/min/mg
Citrobacter braakii
1.9
-
D-glucose 6-phosphate
Vmax: 2.2 micromol/min/mg
Citrobacter braakii
5.12
-
D-glucose 1-phosphate
Vmax: 1.9 micromol/min/mg
Citrobacter braakii
9
-
D-mannose 6-phosphate
Vmax: 2.6 micromol/min/mg
Citrobacter braakii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
43710
-
calculated from cDNA
Citrobacter braakii
46000
-
SDS-PAGE
Citrobacter braakii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Citrobacter braakii
D3GGN3
-
-
Purification (Commentary)
Commentary
Organism
(NH4)2SO4 precipitation, DEAE-sepharose chromatography, CM-sepharose chromatography and FPLC chromatography
Citrobacter braakii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-fructose 6-phosphate + H2O
-
704914
Citrobacter braakii
D-fructose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
-
704914
Citrobacter braakii
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
-
704914
Citrobacter braakii
D-glucose + phosphate
-
-
-
?
D-mannose 6-phosphate + H2O
-
704914
Citrobacter braakii
D-mannose + phosphate
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
45
-
assay at and optimal temperature
Citrobacter braakii
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
55
-
enzyme ist stable up to 55C 30 min
Citrobacter braakii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
assay at and optimal pH
Citrobacter braakii
pH Range
pH Minimum
pH Maximum
Commentary
Organism
3.5
7.5
-
Citrobacter braakii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.5
-
D-glucose 6-phosphate
Vmax: 0.8 micromol/min/mg
Citrobacter braakii
1.9
-
D-glucose 6-phosphate
Vmax: 2.2 micromol/min/mg
Citrobacter braakii
5.12
-
D-glucose 1-phosphate
Vmax: 1.9 micromol/min/mg
Citrobacter braakii
9
-
D-mannose 6-phosphate
Vmax: 2.6 micromol/min/mg
Citrobacter braakii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
43710
-
calculated from cDNA
Citrobacter braakii
46000
-
SDS-PAGE
Citrobacter braakii
Purification (Commentary) (protein specific)
Commentary
Organism
(NH4)2SO4 precipitation, DEAE-sepharose chromatography, CM-sepharose chromatography and FPLC chromatography
Citrobacter braakii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-fructose 6-phosphate + H2O
-
704914
Citrobacter braakii
D-fructose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
-
704914
Citrobacter braakii
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
-
704914
Citrobacter braakii
D-glucose + phosphate
-
-
-
?
D-mannose 6-phosphate + H2O
-
704914
Citrobacter braakii
D-mannose + phosphate
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
45
-
assay at and optimal temperature
Citrobacter braakii
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
55
-
enzyme ist stable up to 55C 30 min
Citrobacter braakii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
assay at and optimal pH
Citrobacter braakii
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
3.5
7.5
-
Citrobacter braakii
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
-
5
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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
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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
-
-
-
-
-
-
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704914
Kim
Purification, characterization ...
Citrobacter braakii
J. Gen. Appl. Microbiol.
55
345-350
2009
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4
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2
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6
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1
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1
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1
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4
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1
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691563
Greiner
-
Production of D-myo-inositol(1 ...
Pantoea agglomerans
Braz. Arch. Biol. Technol.
51
235-246
2008
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-
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
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1
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3
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2
1
1
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1
1
1
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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
-
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
-
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3
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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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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
J. Biol. Chem.
278
31412-31418
2003
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1
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6
1
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2
-
2
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9
-
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6
3
3
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1
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6
1
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2
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9
-
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6
3
3
-
-
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-
-
-
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-
649158
Jia
Purification, crystallization ...
Escherichia coli
Acta Crystallogr. Sect. D
57
314-316
2001
-
-
-
1
-
-
-
-
2
-
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
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1
8
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15
-
1
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7
1
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1
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5
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9
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3
1
6
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1
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1
8
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15
-
1
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7
1
-
1
-
-
-
-
-
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134583
Konichev
-
Metabolic role of the multiple ...
Bombyx mori
Biochemistry
62
543-550
1997
-
-
-
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-
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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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6
3
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1
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3
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7
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-
4
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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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134577
Dassa
The complete nucleotide sequen ...
Escherichia coli
J. Bacteriol.
172
5497-5500
1990
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1
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134578
Pradel
Nucleotide Sequence and Transc ...
Escherichia coli
J. Bacteriol.
172
802- 807
1990
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1
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1
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1
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134576
Pradel
Acid phosphatases of Escherich ...
Escherichia coli
J. Bacteriol.
170
4916
1988
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-
1
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-
7
1
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1
6
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3
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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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134581
Saugy
Phosphatases and phosphodieste ...
Pisum sativum
Eur. J. Biochem.
177
135- 138
1988
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5
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134584
Ching
Acid phosphatases and seed shr ...
Triticosecale Wittmack
Plant Physiol.
76
478-482
1984
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1
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134580
Turner
The hydrolysis of glucose mono ...
Pisum sativum
Biochem. J.
74
486-491
1960
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5
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2
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11
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1
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134582
Faulkner
A hexose-1-phosphatase in silk ...
Bombyx mori
Biochem. J.
60
590-596
1955
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4
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16
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