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Information on EC 3.1.3.25 - inositol-phosphate phosphatase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57573
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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: Methanocaldococcus jannaschii
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
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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-
-
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MJ0109
myo-inositol 1 (or 4) -monophosphatase
-
-
-
-
myo-inositol 1-phosphatase
-
-
-
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Myo-inositol monophosphatase A2
-
-
-
-
myo-inositol-1(or 4)-phosphate phosphohydrolase
-
-
-
-
additional information
IMPase
-
-
-
-
inositol monophosphatase
-
-
-
-
inositol phosphatase
-
-
-
-
MJ0109
-
exhibits NADP(H) phosphatase and fructose-1,6-bisphosphatase activities in addition to the inositol monophosphatase activity, but not 3'-phosphoadenosine 5'-phosphate phosphatase activity
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
additional information
-
archeal enzyme displays inositol monophosphatase as well as fructose 1,6-bisphosphatase activity
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
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
high rate of hydrolysis
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-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
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
600% of the rate with inositol 1-phosphate
-
?
2'-AMP + H2O
adenosine + phosphate
600% of the rate with inositol 1-phosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
very effective substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
very effective substrate
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
-
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
very effective substrate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
very effective substrate
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
16% of the rate with inositol 1-phosphate
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
16% of the rate with inositol 1-phosphate
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + 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
does not contain inositol-containing lipids, involved in biosynthesis of di-myo-inositol-1,1'-phosphate, that serves as osmolyte in hypertermophilic archea
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
organism do not contain lipids with inositol head group, involved in the response to thermal stress
-
?
myo-inositol 2-phosphate + H2O
myo-inositol + phosphate
15% of the rate with inositol 1-phosphate
-
?
myo-inositol 2-phosphate + H2O
myo-inositol + phosphate
15% of the rate with inositol 1-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
-
-
-
-
?
additional information
?
-
D-glucose 6-phosphate, D-fructose 6-phosphate, 5'-AMP and NAD+ are not hydrolyzed
-
?
additional information
?
-
-
D-glucose 6-phosphate, D-fructose 6-phosphate, 5'-AMP and NAD+ are not hydrolyzed
-
?
additional information
?
-
D-glucose 6-phosphate, D-fructose 6-phosphate, 5'-AMP and NAD+ are not hydrolyzed
-
?
additional information
?
-
-
D-glucose 6-phosphate, D-fructose 6-phosphate, 5'-AMP and NAD+ are not hydrolyzed
-
?
additional information
?
-
-
the organism does not accumulate di-myo-inositol 1,1'-phosphate at temperatures above 80°C
-
-
?
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
-
-
?
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-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
very effective substrate
-
?
additional information
?
-
-
the organism does not accumulate di-myo-inositol 1,1'-phosphate at temperatures above 80°C
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
does not contain inositol-containing lipids, involved in biosynthesis of di-myo-inositol-1,1'-phosphate, that serves as osmolyte in hypertermophilic archea
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
organism do not contain lipids with inositol head group, involved in the response to thermal stress
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Li+
Mg2+
additional information
-
metal coordination and binding structures of MJ0109, metal 1 is coordinated by Asp84, Asp201, and two phosphate oxygens from substrate or product in a tetrahedral conformation. Metal 2 is coordinated by Asp84, Asp81, Glu65, a phosphate oxygen, and a water molecule. Metal 3 binding involves Asp38, detailed overview
Mg2+
-
the enzyme requires 5-10 mM Mg21 for optimum catalysis, three to four ions are tightly bound in the absence of ligands. Asp38 coordinates the third metal ion in the substrate complex, but with sufficient flexibility in the loop such that other acidic residues can position the Mg2+ in the active site in the absence of Asp38. Thermodynamic parameters for Mg2+ binding, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mg2+
-
tight binding of Mg2+ to the protein affects the secondary structure
Li+
-
specific mode of action for lithium inhibition in the IMPase superfamily, lithium ion inhibition of the archaeal IMPase is very poor with an IC50 of about 250 mM, mutant D38A enzyme has a dramatically enhanced sensitivity to Li+ with an IC50 of 12 mM
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, kinetic analysis
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12
Li+
Methanocaldococcus jannaschii
-
mutant D38A, pH not specified in the publication, 85°C
240
Li+
Methanocaldococcus jannaschii
-
wild-type enzyme, pH not specified in the publication, 85°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
hanging drop vapor diffusion method, in presence of Ca2+, Zn2+ and substrate or product
hanging drop vapour diffusion method, best crystals in the presence of Zn2+ and phosphate
MJ0109 with bound metal ions, Mg2+, Zn2+, or Mn2+, crystal structure analysis, PDB ID 1DK4
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D26A
-
site-directed mutagenesis, the mutant shows no significant change in the Mg2+ requirement for optimal activity
D38A
-
site-directed mutagenesis, the mutant shows an increased Km for Mg2+, but little effect on kcat compared to the wild-type enzyme, the mutant has a dramatically enhanced sensitivity to Li+ compared to the wild-type, with an IC50 of 12 mM. Electron density map for MJ0109 D38A mobile loop and active site with and without bound Li+, overview
E39A
-
site-directed mutagenesis, the mutant shows no significant change in the Mg2+ requirement for optimal activity
E41A
-
site-directed mutagenesis, the mutant shows no significant change in the Mg2+ requirement for optimal activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the archaeal IMPase is extremely stable and active over a wide temperature range
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 85°C and QFF resin chromatography
-
Toyopearl Super Q-650S column chromatography, phenyl-Sepharose column chromatography, ultracentrifugation, and Sephacryl S-200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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.
Cloning and expression of the inositol monophosphatase gene from Methanococcus jannaschii and characterization of the enzyme
Appl. Environ. Microbiol.
64
2609-2615
1998
Methanocaldococcus jannaschii
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
Johnson, K.A.; Chen, L.; Yang, H.; Roberts, M.F.; Stec, B.
Crystal structure and catalytic mechanism of the MJ0109 gene product: A bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities
Biochemistry
40
618-630
2001
Methanocaldococcus jannaschii (Q57573), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57573)
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
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
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