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Information on EC 3.1.3.25 - inositol-phosphate phosphatase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O30298
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3.1.3.25 inositol-phosphate phosphataseIUBMB Comments
Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. It also acts on adenosine 2'-phosphate (but not the 3'- or 5'- phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate. Two isoforms are known .
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Word Map
- 3.1.3.25
- phosphatidylinositol
-
bipolar
- li+
- phosphoinositide
- sh2
- polyphosphate
-
mood
-
5-phosphatase
- ship-1
-
manic-depressive
- manic
- kinase-3
-
3,4,5-trisphosphate
-
3hinositol
-
mood-stabilizing
-
itims
-
immunoreceptor
-
2-containing
-
tyrosine-based
-
polyphosphoinositide
-
lithium-induced
- 1,4-bisphosphate
-
fcgammariib
-
ptdins
-
lithium-treated
-
pilocarpine-induced
-
coligation
-
ptdins3,4,5p3
- drug development
- pharmacology
- medicine
- synthesis
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
inositol monophosphatase, impase, inositol phosphatase, impa2, impa1, myo-inositol monophosphatase, inpp5f, impp, myo-inositol-1-phosphatase, inositol-1-phosphatase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AF2372
I-1-Pase
-
-
-
-
IMP
-
-
-
-
IMPase
inositol 1-phosphate phosphatase
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-
-
-
inositol monophosphatase
-
-
-
-
inositol monophosphate phosphatase
-
-
-
-
inositol phosphatase
-
-
-
-
inositol phosphohydrolase
-
-
-
-
inositol-1(or 4)-monophosphatase
-
-
-
-
inositol-1-phosphatase
-
-
-
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L-myo-inositol-1-phosphate phosphatase
-
-
-
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Lithium-sensitive myo-inositol monophosphatase A1
-
-
-
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myo-inositol 1 (or 4) -monophosphatase
-
-
-
-
myo-inositol 1-phosphatase
-
-
-
-
Myo-inositol monophosphatase A2
-
-
-
-
myo-inositol-1(or 4)-phosphate phosphohydrolase
-
-
-
-
AF2372
exhibits NADP(H) phosphatase and fructose-1,6-bisphosphatase activities in addition to inositol monophosphatase activitity, but not 3'-phosphoadenosine 5'-phosphate phosphatase activity
IMPase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
myo-inositol phosphate + H2O = myo-inositol + phosphate
the active site residues Tyr155, Glu175, Asp85, and Ser171 are required for the hydrogen bond network in the active site
myo-inositol phosphate + H2O = myo-inositol + phosphate
catalytic mechanism and stereospecificity
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
myo-inositol-phosphate phosphohydrolase
Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. It also acts on adenosine 2'-phosphate (but not the 3'- or 5'- phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate. Two isoforms are known [4].
CAS REGISTRY NUMBER
COMMENTARY
37184-63-7
-
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
3,5-dideoxy-D-myo-inositol 1-phosphate + H2O
3,5-dideoxy-D-myo-inositol + phosphate
-
-
-
?
3,5-dideoxy-L-myo-inositol 1-phosphate + H2O
3,5-dideoxy-L-myo-inositol + phosphate
-
-
-
?
D-myo-inositol 2-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
3,5-dideoxy-D-myo-inositol 1-phosphate + H2O
3,5-dideoxy-D-myo-inositol + phosphate
-
-
-
-
?
3,5-dideoxy-L-myo-inositol 1-phosphate + H2O
3,5-dideoxy-L-myo-inositol + phosphate
-
-
-
-
?
3-deoxy-D-myo-inositol 1-phosphate + H2O
3-deoxy-D-myo-inositol + phosphate
-
-
-
-
?
3-deoxy-L-myo-inositol 1-phosphate + H2O
3-deoxy-L-myo-inositol + phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
substrate binding structure, interactions sites with the enzyme involving Tyr155 and Ala172
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
very effective substrate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
very effective substrate
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
organism do not contain lipids with inositol head group, involved in the response to thermal stress
-
?
additional information
?
-
at temperatures above 80°C the organism accumulates di-myo-inositol 1,1'-phosphate as a compatible solute which is regulated by the temperature dependence of the substrate affinity
-
-
?
additional information
?
-
-
at temperatures above 80°C the organism accumulates di-myo-inositol 1,1'-phosphate as a compatible solute which is regulated by the temperature dependence of the substrate affinity
-
-
?
additional information
?
-
the enzyme also shows low fructose bisphosphatase activity
-
-
?
additional information
?
-
-
the enzyme also shows low fructose bisphosphatase activity
-
-
?
additional information
?
-
D-myo-inositol-1,4,5-triphosphate, D-glucose 6-phosphate, D-fructose 6-phosphate, NAD+, FMN+, bis-p-nitrophenyl diphosphate, ADP and ATP are no substrates
-
-
?
additional information
?
-
-
D-myo-inositol-1,4,5-triphosphate, D-glucose 6-phosphate, D-fructose 6-phosphate, NAD+, FMN+, bis-p-nitrophenyl diphosphate, ADP and ATP are no substrates
-
-
?
additional information
?
-
the enzyme also exhibits high phosphatase activities toward NADP(H) and toward 2'-AMP and 2'-phosphoadenosine 5'-phosphate, but not toward 3'-AMP, 3'-phosphoadenosine 5'-phosphate, and 5'-AMP
-
-
?
additional information
?
-
-
the enzyme also exhibits high phosphatase activities toward NADP(H) and toward 2'-AMP and 2'-phosphoadenosine 5'-phosphate, but not toward 3'-AMP, 3'-phosphoadenosine 5'-phosphate, and 5'-AMP
-
-
?
additional information
?
-
-
archeal enzyme displays inositol monophosphatase as well as fructose 1,6-bisphosphatase activity
-
?
additional information
?
-
-
archeal enzyme displays inositol monophosphatase as well as fructose 1,6-bisphosphatase activity
-
?
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
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
very effective substrate
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
organism do not contain lipids with inositol head group, involved in the response to thermal stress
-
?
additional information
?
-
at temperatures above 80°C the organism accumulates di-myo-inositol 1,1'-phosphate as a compatible solute which is regulated by the temperature dependence of the substrate affinity
-
-
?
additional information
?
-
-
at temperatures above 80°C the organism accumulates di-myo-inositol 1,1'-phosphate as a compatible solute which is regulated by the temperature dependence of the substrate affinity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
dependent on, involved in temeprature-dependent substrate affinity regulation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O2
-
activity of the native enzyme but not the C150S mutant can be completely abolished with oxygen, reversible with thiol-containing compounds
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme is not upregulated upon thermal stress
-
additional information
-
the enzyme is not upregulated upon thermal stress
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
analysis of temperature-dependence of the Km value of inositol 1-phosphate substrates, the enzyme's fructose bisphosphatase activity is temperature independent between 55°C and 70°C, but fructose bisphosphate is not stable above 70°C
-
additional information
additional information
-
analysis of temperature-dependence of the Km value of inositol 1-phosphate substrates, the enzyme's fructose bisphosphatase activity is temperature independent between 55°C and 70°C, but fructose bisphosphate is not stable above 70°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
3,5-dideoxy-L-myo-inositol 1-phosphate
pH 8.0, 85°C
additional information
3,5-dideoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 85°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55 - 85
the activity increases with increasing temperature, temperature profile
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized by vapor diffusion using hanging drops of 0.005 ml. The apoenzyme is crystallized in either 0.2 M ammonium nitrate and 30% PEG 3350 or 0.2 M dihydrogen ammonium phosphate and 30% PEG 3350
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S171A
site-directed mutagenesis, mutation of an active site residue involved in hydrogen bonding, the mutant shows impaired Mg2+ binding, weak substrate binding at all temperatures, and no change in Km with increasing temperature in contrast to the wild-type enzyme
T174L
site-directed mutagenesis, mutation of an active site residue involved in hydrogen bonding, the mutant shows no change in Km with increasing temperature in contrast to the wild-type enzyme
C150S
-
insensitive toward inactivation with oxygen or thioredoxin, no effect on activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by heat treatment at 85°C and QFF resin chromatography
Toyopearl Super Q-650S column chromatography, ultracentrifugation, and Sephacryl S-200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expressed in Eschericha coli inositol monophosphatase deficient strain CG1307, can not complement effects of inositol monophosphatase deficiency
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, L.; Roberts, M.F.
Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: Comparison with bacterial and archaeal inositol monophosphatases
Biochemistry
39
4145-4153
2000
Archaeoglobus fulgidus, Escherichia coli, Methanocaldococcus jannaschii, Thermotoga maritima
Stec, B.; Yang, H.; Johnson, K.A.; Chen, L.; Roberts, M.F.
MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase
Nat. Struct. Biol.
7
1046-1050
2000
Archaeoglobus fulgidus, Escherichia coli, Thermotoga maritima, Methanocaldococcus jannaschii (Q57573), Methanocaldococcus jannaschii, Thermotoga maritima TM1415, Archaeoglobus fulgidus AF2372
Stieglitz, K.A.; Seaton, B.A.; Head, J.F.; Stec, B.; Roberts, M.F.
Unexpected similarity in regulation between an archaeal inositol monophosphatase/fructose bisphosphatase and chloroplast fructose bisphosphatase
Protein Sci.
12
760-767
2003
Archaeoglobus fulgidus, Archaeoglobus fulgidus AF2372, Methanocaldococcus jannaschii, Methanocaldococcus jannaschii MJ0109
Wang, Y.K.; Morgan, A.; Stieglitz, K.; Stec, B.; Thompson, B.; Miller, S.J.; Roberts, M.F.
The temperature dependence of the inositol monophosphatase Km correlates with accumulation of di-myo-inositol 1,1'-phosphate in Archaeoglobus fulgidus
Biochemistry
45
3307-3314
2006
Archaeoglobus fulgidus (O30298), Archaeoglobus fulgidus, Methanocaldococcus jannaschii, Thermotoga maritima
Morgan, A.J.; Wang, Y.K.; Roberts, M.F.; Miller, S.J.
Chemistry and biology of deoxy-myo-inositol phosphates: stereospecificity of substrate interactions within an archaeal and a bacterial IMPase
J. Am. Chem. Soc.
126
15370-15371
2004
Archaeoglobus fulgidus, Escherichia coli
Fukuda, C.; Kawai, S.; Murata, K.
NADP(H) phosphatase activities of archaeal inositol monophosphatase and eubacterial 3-phosphoadenosine 5-phosphate phosphatase
Appl. Environ. Microbiol.
73
5447-5452
2007
Archaeoglobus fulgidus (O30298), Archaeoglobus fulgidus, Escherichia coli, Methanocaldococcus jannaschii
Stieglitz, K.A.; Johnson, K.A.; Yang, H.; Roberts, M.F.; Seaton, B.A.; Head, J.F.; Stec, B.
Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop
J. Biol. Chem.
277
22863-22874
2002
Archaeoglobus fulgidus (O30298), Archaeoglobus fulgidus
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