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3-phosphoglycerate + H2O
2,3-dihydroxypropanoic acid + phosphate
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
ADP + H2O
AMP + phosphate
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
AMP + H2O
adenosine + phosphate
ATP + H2O
ADP + phosphate
beta-glyceryl phosphate + H2O
glycerol + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
D-fructose 1-phosphate + H2O
D-fructose + phosphate
D-fructose 6-phosphate + H2O
D-fructose + phosphate
D-galactose 1-phosphate + H2O
D-galactose + phosphate
D-glucose 1-phosphate + H2O
D-glucose + phosphate
D-glucose 6-phosphate
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
D-mannose 6-phosphate + H2O
D-mannose + phosphate
-
-
-
?
D-ribose 5-phosphate
D-ribose + phosphate
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
diphosphate + H2O
2 phosphate
-
-
-
?
fructose 1-phosphate
fructose + phosphate
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
glycerol 3-phosphate + H2O
glycerol + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
myo-inositol hexakisphosphate + H2O
D-myo-inositol(1,2,4,5,6)pentakisphosphate + phosphate
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
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
-
-
?
additional information
?
-
3-phosphoglycerate + H2O
2,3-dihydroxypropanoic acid + phosphate
-
-
-
?
3-phosphoglycerate + H2O
2,3-dihydroxypropanoic acid + phosphate
-
hydrolysis is more rapid than that of glucose monophosphates
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
hydrolysis is more rapid than that of glucose monophosphate
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
high activity
-
-
?
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
high activity
-
-
?
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
high activity
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
high activity
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
AMP + H2O
adenosine + phosphate
-
enzyme form GP3 of the fat body is inactive with AMP
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
enzyme forms GP3 and GP3'
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
hydrolysis more rapid than that of glucose monophosphates
-
?
ATP + H2O
ADP + phosphate
Triticosecale Wittmack
-
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
-
-
-
r
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
-
hydrolysis was more rapid than that of glucose monophosphates
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
r
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
r
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-galactose 1-phosphate + H2O
D-galactose + phosphate
-
-
-
?
D-galactose 1-phosphate + H2O
D-galactose + phosphate
-
-
-
-
ir
D-galactose 1-phosphate + H2O
D-galactose + phosphate
-
-
-
r
D-galactose 1-phosphate + H2O
D-galactose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
-
ir
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
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
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
r
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
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 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
Triticosecale Wittmack
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
no catalysis
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
r
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
the enzyme acts as a D-glucose scavenger
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
enzyme is only able to cleave off the third phosphate group of myo-inositol
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
-
-
?
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme is potentially involved in pathogenic inositol phosphate signal transduction pathways via type III secretioin into the host cell
-
?
additional information
?
-
-
the enzyme hydrolyzes a wide variety of phosphorylated compounds, primarily small monosaccharide phosphates, overview
-
-
?
additional information
?
-
-
the enzyme hydrolyzes a wide variety of phosphorylated compounds, primarily small monosaccharide phosphates, overview
-
-
?
additional information
?
-
the bifunctional enzyme also exhibits 3-phytase activity, cf. EC 3.1.3.8
-
-
?
additional information
?
-
glucose-1-phosphatase enzymes and, specifically, Agp phytases are known to have a broad substrate specificity. The bifunctional enzyme from Pantoea sp. 3.5.1 also exhibits 3-phytase activity, cf. EC 3.1.3.8. Broad substrate specificity, substrates are phytate and many other phosphate-containing substrates, such as AMP, NADP, pNPP, 1-naphthyl phosphate, glucose phosphates, beta-glycerol phosphate, and diphosphate, overview
-
-
?
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alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
D-fructose 1-phosphate + H2O
D-fructose + phosphate
D-fructose 6-phosphate + H2O
D-fructose + phosphate
D-galactose 1-phosphate + H2O
D-galactose + phosphate
D-glucose 1-phosphate + H2O
D-glucose + phosphate
D-glucose 6-phosphate + H2O
D-glucose + phosphate
D-ribose 5-phosphate + H2O
D-ribose + phosphate
myo-inositol hexakisphosphate + H2O
? + phosphate
-
the enzyme is potentially involved in pathogenic inositol phosphate signal transduction pathways via type III secretioin into the host cell
-
?
additional information
?
-
the bifunctional enzyme also exhibits 3-phytase activity, cf. EC 3.1.3.8
-
-
?
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
high activity
-
-
?
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
high activity
-
-
?
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
high activity
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
high activity
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
-
-
-
r
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
r
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
r
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-galactose 1-phosphate + H2O
D-galactose + phosphate
-
-
-
-
?
D-galactose 1-phosphate + H2O
D-galactose + phosphate
-
-
-
-
ir
D-galactose 1-phosphate + H2O
D-galactose + phosphate
-
-
-
r
D-galactose 1-phosphate + H2O
D-galactose + phosphate
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
-
ir
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
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
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
r
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
Triticosecale Wittmack
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
r
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
the enzyme acts as a D-glucose scavenger
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
-
?
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(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
iodoacetic acid
-
69% inhibition of D-glucose 1-phosphate hydrolysis by 10 mM
Na3As04
-
85% inhibition of D-glucose 1-phosphate hydrolysis by 10 mM
Na3VO4
-
50% inhibition of membrane bound activity by 0.1 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
HgCl2
-
99% inhibition of 4-nitrophenyl phosphate hydrolysis by 10 mM
HgCl2
-
74% inhibition of D-glucose 1-phosphate hydrolysis by 0.2 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
NaF
-
56% inhibition of D-glucose 1-phosphate hydrolysis by 0.2 mM
NaF
-
no inhibition through NaF for the acid phosphatase AP35
NaF
-
75% inhibition of D-glucose 1-phosphate hydrolysis by 2.0 mM, 100% inhibition of D-glucose 1-phosphate hydrolysis by 20 mM
phosphate
-
54% inhibition of D-glucose 1-phosphate hydrolysis by 10 mM
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
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142
-
substrate D-fructose 1-phosphate, 37°C, pH 5.0
146
-
substrate D-glucose 1-phosphate, 37°C, pH 5.0
159
-
substrate D-glucose 6-phosphate, 37°C, pH 5.0
196
-
substrate D-glucose 1-phosphate, 37°C, pH 5.0
32
-
substrate myo-inositol hexakisphosphate, 37°C, pH 5.0
5.92
purified recombinant His-tagged enzyme, pH and temperature not specified in the publication, substrate alpha-D-glucose 1-phosphate
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
100
-
with D-fructose 6-phosphate as substrate, purification procedure described
100
-
purification procedure described
100
-
with D-glucose 1-phosphate as substrate
130
-
purification procedure described
130
-
with D-fructose 1-phosphate as substrate
2090
-
purification procedure described
2090
-
with D-galactose 1-phosphate as substrate
210
-
purification procedure described
210
-
with adenosine diphosphate as substrate
2360
-
purification procedure described
2360
-
with D-glucose 1-phosphate as substrate
30
-
with ribose 5-phosphate as substrate, purification procedure described
30
-
with nitrophenyl phosphate as substrate, purification procedure described
40
-
substrate D-fructose 6-phosphate, 37°C, pH 5.0
40
-
with phosphoenolpyruvate as substrate
40
-
purification procedure described
410
-
purification procedure described
410
-
with adenosine triphosphate as substrate
637
-
purification procedure described
637
-
with D-glucose 6-phosphate as substrate
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Pradel, E.; Boquet, P.L.
Acid phosphatases of Escherichia coli: molecular cloning and analysis of agp, the structural gene for a periplasmic acid glucose phosphatase
J. Bacteriol.
170
4916
1988
Escherichia coli
brenda
Dassa, J.; Marck, C.; Boquet, P.L.
The complete nucleotide sequence of the Escherichia coli gene appA reveals significant homology between pH 2.5 acid phosphatase and glucose-1-phosphatase
J. Bacteriol.
172
5497-5500
1990
Escherichia coli
brenda
Pradel, E.; Marck, Ch.; Boqet, P.L.
Nucleotide Sequence and Transcriptional Analysis of the Escherichia coli agp Gene Encoding Periplasmic Acid Glucose-1-Phosphatase
J. Bacteriol.
172
802- 807
1990
Escherichia coli
brenda
Pradel, E.; Boquet, P.L.
Utilization of exogenous glucose-1-phosphate as a source of carbon or phosphate by Escherichia coli K12: respective roles of acid glucose-1-phosphatase, hexose-phosphate permease, phosphoglucomutase and alkaline phosphatase
Res. Microbiol.
142
37- 45
1991
Escherichia coli
brenda
Turner, D.H.; Turner, J.F.
The hydrolysis of glucose monophosphates by a phosphatase preparation from pea seeds
Biochem. J.
74
486-491
1960
Pisum sativum
brenda
Saugy, M.; Farkas, V.; MacLachlan, G.
Phosphatases and phosphodiesterases interfere with 1,3-(-D)-glucan synthase activity in pea epicotyl membrane preparations
Eur. J. Biochem.
177
135- 138
1988
Pisum sativum
brenda
Faulkner, P.
A hexose-1-phosphatase in silkworm blood
Biochem. J.
60
590-596
1955
Bombyx mori
brenda
Konichev, A.S.
Metabolic role of the multiple forms of glucose-1-phosphatase, NAD+-and NADP+-dependent sorbitol dehydrogenases, acid phosphatase, and glucose-6-phosphate dehydrogenase in tissues and organs of the silkworm
Biochemistry
62
543-550
1997
Bombyx mori
-
brenda
Ching, T.M.; Thompson, D.M.; Metzger, R.J.
Acid phosphatases and seed shriveling in triticale
Plant Physiol.
76
478-482
1984
Triticosecale Wittmack
brenda
Joh, T.; Yazaki, J.; Suzuki, K.; Hayakawa, T.
Isolation and properties of glucose-1-phosphatase from mycelia of Pholiota nemako
Biosci. Biotechnol. Biochem.
62
2251-2253
1998
Pholiota nameko
brenda
Jia, Z.; Cottrill, M.; Pal, G.P.; Lee, D.; Sung, M.; Forsberg, C.W.; Phillips, J.P.
Purification, crystallization and preliminary X-ray analysis of the Escherichia coli glucose-1-phosphatase
Acta Crystallogr. Sect. D
57
314-316
2001
Escherichia coli
brenda
Lee, D.C.; Cottrill, M.A.; Forsberg, C.W.; Jia, Z.
Functional insights revealed by the crystal structures of Escherichia coli glucose-1-phosphatase
J. Biol. Chem.
278
31412-31418
2003
Escherichia coli
brenda
Herter, T.; Berezina, O.V.; Zinin, N.V.; Velikodvorskaya, G.A.; Greiner, R.; Borriss, R.
Glucose-1-phosphatase (AgpE) from Enterobacter cloacae displays enhanced phytase activity
Appl. Microbiol. Biotechnol.
70
60-64
2006
Enterobacter cloacae
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Greiner, R.; Sajidan, S.
Production of D-myo-inositol(1,2,4,5,6)pentakisphosphate using alginate-entrapped recombinant Pantoea agglomerans glucose-1-phosphatase
Braz. Arch. Biol. Technol.
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2008
Pantoea agglomerans (Q1W5Y8)
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Kim, Y.O.; Kim, H.W.; Park, I.S.; Lee, J.H.; Lee, S.J.; Kim, K.K.
Purification, characterization, and gene cloning of glucose-1-phosphatase from Citrobacter braakii
J. Gen. Appl. Microbiol.
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345-350
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Citrobacter braakii (D3GGN3), Citrobacter braakii
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Kim, Y.; Park, I.; Nam, B.; Kong, H.; Kim, W.; Lee, S.; Kim, K.
Gene cloning, expression, and characterization of glucose-1-phosphatase from Enterobacter cloacae B11
Fish. Aqua. Sci.
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Enterobacter cloacae, Enterobacter cloacae B11
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Suleimanova, A.D.; Beinhauer, A.; Valeeva, L.R.; Chastukhina, I.B.; Balaban, N.P.; Shakirov, E.V.; Greiner, R.; Sharipova, M.R.
Novel glucose-1-phosphatase with high phytase activity and unusual metal ion activation from soil bacterium Pantoea sp. strain 3.5.1
Appl. Environ. Microbiol.
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6790-6799
2015
Pantoea sp. 3.5.1 (A0A075FFV0)
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