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Information on EC 3.1.3.10 - glucose-1-phosphatase
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3.1.3.10 glucose-1-phosphataseIUBMB Comments
Also acts, more slowly, on D-galactose 1-phosphate.
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Word Map
- 3.1.3.10
- phosphatases
- dsba
- appa
- myo-inositol
-
cryoprotectant
- silkworm
- enterobacter
- 3-phytase
- phytases
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glucose-1-phosphatase, acid glucose-1-phosphatase, g-1-pase, periplasmic acid glucose-1-phosphatase, g1pase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid glucose-1-phosphatase
acid phosphatase
AGP
G-1-Pase
G1Pase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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-
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose-1-phosphate phosphohydrolase
Also acts, more slowly, on D-galactose 1-phosphate.
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CAS REGISTRY NUMBER
COMMENTARY
9001-38-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
?
3-phosphoglycerate + H2O
2,3-dihydroxypropanoic acid + phosphate
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hydrolysis is more rapid than that of glucose monophosphates
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
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hydrolysis is more rapid than that of glucose monophosphate
-
?
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
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high activity
-
-
?
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
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high activity
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
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high activity
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
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high activity
-
-
?
AMP + H2O
adenosine + phosphate
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enzyme form GP3 of the fat body is inactive with AMP
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-
?
ATP + H2O
ADP + phosphate
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hydrolysis more rapid than that of glucose monophosphates
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose + phosphate
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hydrolysis was more rapid than that of glucose monophosphates
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?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
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multiple forms of glucose-1-phosphatase specify for glucose 1-phosphate and galactose 1-phosphate in hemolymph of the silkworm
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-
ir
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
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-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
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the enzyme acts as a D-glucose scavenger
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?
myo-inositol hexakisphosphate + H2O
? + phosphate
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enzyme is only able to cleave off the third phosphate group of myo-inositol
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?
myo-inositol hexakisphosphate + H2O
? + phosphate
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the enzyme is potentially involved in pathogenic inositol phosphate signal transduction pathways via type III secretioin into the host cell
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?
additional information
?
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the enzyme hydrolyzes a wide variety of phosphorylated compounds, primarily small monosaccharide phosphates, overview
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?
additional information
?
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the enzyme hydrolyzes a wide variety of phosphorylated compounds, primarily small monosaccharide phosphates, overview
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?
additional information
?
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the bifunctional enzyme also exhibits 3-phytase activity, cf. EC 3.1.3.8
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?
additional information
?
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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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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
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the bifunctional enzyme also exhibits 3-phytase activity, cf. EC 3.1.3.8
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-
?
alpha-D-glucose 1-phosphate + H2O
D-glucose + phosphate
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high activity
-
-
?
alpha-D-glucose 1-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
-
high activity
-
-
?
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 6-phosphate + H2O
D-glucose + phosphate
-
the enzyme acts as a D-glucose scavenger
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)6Mo7O24
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98% inhibition of 4 -nitrophenyl phosphate hydrolysis by 1.0 mM
tartaric acid
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36% inhibition of 4-nitrophenyl phosphate hydrolysis by 10 mM
NaF
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75% inhibition of D-glucose 1-phosphate hydrolysis by 2.0 mM, 100% inhibition of D-glucose 1-phosphate hydrolysis by 20 mM
phosphate
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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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.24
alpha-D-glucose 1-phosphate
recombinant His-tagged enzyme, pH and temperature not specified in the publication