Information on EC 3.1.3.25 - inositol-phosphate phosphatase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY
3.1.3.25
-
RECOMMENDED NAME
GeneOntology No.
inositol-phosphate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
myo-inositol phosphate + H2O = myo-inositol + phosphate
show the reaction diagram
-
-
-
-
myo-inositol phosphate + H2O = myo-inositol + phosphate
show the reaction diagram
the catalytic mechanism involves three Mg2+ ions, modeling of the reaction and the postreaction complex, active site structure, substrate binding structure, overview
P20456
myo-inositol phosphate + H2O = myo-inositol + phosphate
show the reaction diagram
enzyme is both inositol monophosphatase and fructose-1,6-bisphosphatase
-
myo-inositol phosphate + H2O = myo-inositol + phosphate
show the reaction diagram
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
show the reaction diagram
catalytic mechanism and stereospecificity
-
myo-inositol phosphate + H2O = myo-inositol + phosphate
show the reaction diagram
catalytic mechanism and substrate-enzyme interactions, active site residues
-
PATHWAY
KEGG Link
MetaCyc Link
D-myo-inositol (1,4,5)-trisphosphate degradation
-
myo-inositol biosynthesis
-
phytate degradation I
-
Streptomycin biosynthesis
-
Inositol phosphate metabolism
-
Metabolic pathways
-
Biosynthesis of secondary metabolites
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AF2372
O30298
exhibits NADP(H) phosphatase and fructose-1,6-bisphosphatase activities in addition to inositol monophosphatase activitity, but not 3'-phosphoadenosine 5'-phosphate phosphatase activity
AF2372
O30298
gene name
I-1-Pase
-
-
-
-
IMP
-
-
-
-
IMP
Q6NPM8, Q94F00, Q9M8S8
-
IMP-1 protein
B3DFH0
-
IMPA1
P29218
-
IMPA2
O14732
-
IMPase
-
-
-
-
IMPase
-
-
IMPase
-
-
IMPase
B3DFH0
-
IMPase
O14732, P29218
-
IMPase
Mycobacterium tuberculosis H37Rv, ATCC 25618
-
-
-
IMPase
Q6G709
-
IMPase
Staphylococcus aureus MSSA476
Q6G709
-
-
IMPase
O33832
-
IMPase/FBPase
-
-
IMPase/FBPase
O30298
-
IMPP
-
-
inositol 1-phosphate phosphatase
-
-
-
-
inositol 1-phosphate phosphatase
O33832
-
inositol monophosphatase
-
-
-
-
inositol monophosphatase
-
-
inositol monophosphatase
Q6NPM8, Q94F00, Q9M8S8
-
inositol monophosphatase
O30298
-
inositol monophosphatase
-
-
inositol monophosphatase
-
-
inositol monophosphatase
-
-
inositol monophosphatase
-
-
inositol monophosphatase
Q6G709
-
inositol monophosphatase
Staphylococcus aureus MSSA476
Q6G709
-
-
inositol monophosphatase
-
-
inositol monophosphatase/fructose-1,6-bisphosphatase
-
-
inositol monophosphate phosphatase
-
-
-
-
inositol monophosphate phosphatase
-
-
inositol monophosphate phosphatase
Mycobacterium tuberculosis H37Rv, ATCC 25618
-
-
-
inositol phosphatase
-
-
-
-
inositol phosphatase
O30298
-
inositol phosphatase
-
-
inositol phosphatase
-
-
inositol phosphatase
-
-
inositol phosphohydrolase
-
-
-
-
inositol-1(or 4)-monophosphatase
-
-
-
-
inositol-1(or 4)-monophosphatase
-
-
inositol-1-phosphatase
-
-
-
-
L-myo-inositol 1-phosphate phosphatase
-
-
L-myo-inositol-1-phosphate phosphatase
-
-
-
-
Lithium-sensitive myo-inositol monophosphatase A1
-
-
-
-
myo-inositol 1 (or 4) -monophosphatase
-
-
-
-
myo-inositol 1 (or 4) monophosphatase
-
-
myo-inositol 1-phosphatase
-
-
-
-
myo-inositol monophosphatase
Q6NPM8, Q94F00, Q9M8S8
-
myo-inositol monophosphatase
-
-
myo-inositol monophosphatase
-
-
myo-inositol monophosphatase
O14732, P29218
-
myo-inositol monophosphatase 1
-
-
myo-inositol monophosphatase 2
-
-
Myo-inositol monophosphatase A2
-
-
-
-
myo-inositol monophosphatase-1
P97697
-
myo-inositol monophosphate phosphatase
-
-
myo-inositol-1(or 4)-phosphate phosphohydrolase
-
-
-
-
myo-inositol-1-phosphatase
-
-
myo-inositol-1-phosphatase/aryl-phosphatase
-
exhibits also Zn-dependent aryl-phosphatase activity at acidic pH
myo-inositol-1-phosphate phosphohydrolase
-
-
myo-inositol-phosphatase
-
-
SAS2203
Q6G709
gene name
SAS2203
Staphylococcus aureus MSSA476
Q6G709
gene name
-
SuhB
O30298
gene name
TM1415
O33832
exhibits dual specificity with both IMPase and fructose-1,6-bisphosphatase activities
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
Methanocaldococcus jannaschii MJ0109
-
archeal enzyme displays inositol monophosphatase as well as fructose 1,6-bisphosphatase activity
-
additional information
Q6G709
the enzyme belongs to the FIG superfamily of proteins
additional information
Staphylococcus aureus MSSA476
Q6G709
the enzyme belongs to the FIG superfamily of proteins
-
CAS REGISTRY NUMBER
COMMENTARY
37184-63-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene Impa1
-
-
Manually annotated by BRENDA team
IMPL1; ecotype Columbia-0, genes IMPL1, IMPL2, and VTC4
UniProt
Manually annotated by BRENDA team
IMPL2; ecotype Columbia-0, genes IMPL1, IMPL2, and VTC4
UniProt
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
VTC4; ecotype Columbia-0, genes IMPL1, IMPL2, and VTC4
UniProt
Manually annotated by BRENDA team
Archaeoglobus fulgidus AF2372
strain AF2372
-
-
Manually annotated by BRENDA team
gene suhB
-
-
Manually annotated by BRENDA team
gene IMPA2
-
-
Manually annotated by BRENDA team
cv. Harrington, wild-type and mutant
SwissProt
Manually annotated by BRENDA team
Methanocaldococcus jannaschii MJ0109
strain MJ0109
-
-
Manually annotated by BRENDA team
IMPA1
SwissProt
Manually annotated by BRENDA team
IMPA2
SwissProt
Manually annotated by BRENDA team
strain MC2 155
-
-
Manually annotated by BRENDA team
Mycobacterium smegmatis MC2 155
strain MC2 155
-
-
Manually annotated by BRENDA team
genes impA or Rv1604, and impC or Rv3137
-
-
Manually annotated by BRENDA team
strain H37Rv, gene Rv2131c
-
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis H37Rv, ATCC 25618
genes impA or Rv1604, and impC or Rv3137
-
-
Manually annotated by BRENDA team
bv. trifolii
-
-
Manually annotated by BRENDA team
stains RS16, RS347, RS1238 and YML89
-
-
Manually annotated by BRENDA team
gene sas2203
UniProt
Manually annotated by BRENDA team
Staphylococcus aureus MSSA476
gene sas2203
UniProt
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
strain TM1415
-
-
Manually annotated by BRENDA team
Thermotoga maritima TM1415
strain TM1415
-
-
Manually annotated by BRENDA team
Methanocaldococcus jannaschii MJ109
strain MJ109
Uniprot
Manually annotated by BRENDA team
additional information
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
existence of three distinct evolutionary groups of enzyme: vertebrate IMPA1 proteins, vertebrate IMPA2 proteins and invertebrate IMPA proteins
malfunction
Q6NPM8, Q94F00, Q9M8S8
the impl2 mutant has an embryo lethal phenotype, while the impl1 and vtc4 mutants do not; the impl2 mutant has an embryo lethal phenotype, while the impl1 and vtc4 mutants do not; the impl2 mutant has an embryo lethal phenotype, while the impl1 and vtc4 mutants do not
metabolism
Q6NPM8, Q94F00, Q9M8S8
myo-inositol monophosphatase catalyzes the dephosphorylation of myo-inositol 3-phosphate in the last step of myo-inositol biosynthesis. Expression of IMP genes is correlated with expression of the gene for myo-inositol polyphosphate 1-phosphatase, which is involved in the myo-inositol salvage pathway, suggesting a possible salvage pathway role in seed development. Moreover, the partial rescue of the impl2 phenotype by histidine application implies that IMPL2 is also involved in histidine biosynthesis during embryo development; myo-inositol monophosphatase catalyzes the dephosphorylation of myo-inositol 3-phosphate in the last step of myo-inositol biosynthesis. Expression of IMP genes is correlated with expression of the gene for myo-inositol polyphosphate 1-phosphatase, which is involved in the myo-inositol salvage pathway, suggesting a possible salvage pathway role in seed development. Moreover, the partial rescue of the impl2 phenotype by histidine application implies that IMPL2 is also involved in histidine biosynthesis during embryo development; myo-inositol monophosphatase catalyzes the dephosphorylation of myo-inositol 3-phosphate in the last step of myo-inositol biosynthesis. Expression of IMP genes is correlated with expression of the gene for myo-inositol polyphosphate 1-phosphatase, which is involved in the myo-inositol salvage pathway, suggesting a possible salvage pathway role in seed development. Moreover, the partial rescue of the impl2 phenotype by histidine application implies that IMPL2 is also involved in histidine biosynthesis during embryo development
physiological function
-
Mycobacteria use inositol in phosphatidylinositol, for anchoring lipoarabinomannan, lipomannan, and phosphatidylinosotol mannosides in the cell envelope, and for the production of mycothiol, which maintains the redox balance of the cell. The protein encoded by gene impA is partly responsible for inositol synthesis, while the impC encoded protein is essential, overview
physiological function
Q6NPM8, Q94F00, Q9M8S8
myo-inositol monophosphatase catalyzes the dephosphorylation of myo-inositol 3-phosphate in the last step of myo-inositol biosynthesis. Myo-inositol monophosphatase is also important in phosphate metabolism and is required for the biosynthesis of cell wall polysaccharides, phytic acid, and phosphatidylinositol; myo-inositol monophosphatase catalyzes the dephosphorylation of myo-inositol 3-phosphate in the last step of myo-inositol biosynthesis. Myo-inositol monophosphatase is also important in phosphate metabolism and is required for the biosynthesis of cell wall polysaccharides, phytic acid, and phosphatidylinositol; myo-inositol monophosphatase catalyzes the dephosphorylation of myo-inositol 3-phosphate in the last step of myo-inositol biosynthesis. Myo-inositol monophosphatase is also important in phosphate metabolism and is required for the biosynthesis of cell wall polysaccharides, phytic acid, and phosphatidylinositol
physiological function
Mycobacterium tuberculosis H37Rv, ATCC 25618
-
Mycobacteria use inositol in phosphatidylinositol, for anchoring lipoarabinomannan, lipomannan, and phosphatidylinosotol mannosides in the cell envelope, and for the production of mycothiol, which maintains the redox balance of the cell. The protein encoded by gene impA is partly responsible for inositol synthesis, while the impC encoded protein is essential, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl cyclohexylammonium 1-hydroxyphosphonate + H2O
?
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
-
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
-
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
18% of the rate with inositol 1-phosphate
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
Q57573
600% of the rate with inositol 1-phosphate
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
Q57573
600% of the rate with inositol 1-phosphate
-
?
2'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
2'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
2'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-phosphoadenosine 5'-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
2'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
2'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
2,3-diphosphoglycerate + H2O
?
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
?
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
?
show the reaction diagram
-
-
-
-
-
2-phosphoglycerol + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
-
2-phosphoglycerol + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
2-phosphoglycolate + H2O
?
show the reaction diagram
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
-
3'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
3'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
3,5-dideoxy-D-myo-inositol 1-phosphate + H2O
3,5-dideoxy-D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
3,5-dideoxy-D-myo-inositol 1-phosphate + H2O
3,5-dideoxy-D-myo-inositol + phosphate
show the reaction diagram
-, O30298
-
-
-
?
3,5-dideoxy-L-myo-inositol 1-phosphate + H2O
3,5-dideoxy-L-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
3,5-dideoxy-L-myo-inositol 1-phosphate + H2O
3,5-dideoxy-L-myo-inositol + phosphate
show the reaction diagram
-, O30298
-
-
-
?
3-deoxy-D-myo-inositol 1-phosphate + H2O
3-deoxy-D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
3-deoxy-L-myo-inositol 1-phosphate + H2O
3-deoxy-L-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
3-phosphoglycerate + H2O
?
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
high rate of hydrolysis
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Q57573
very effective substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Q57573
very effective substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Archaeoglobus fulgidus, Thermotoga maritima, Thermotoga maritima TM1415, Archaeoglobus fulgidus AF2372
-
very effective substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Archaeoglobus fulgidus AF2372
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-dAMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
6-phosphogluconate + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-D-galactose 1-phosphate + H2O
alpha-D-galactose + phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose + phosphate
show the reaction diagram
O14732, P29218
IMPA1 shows intermediate activity towards alpha-D-glucose 1-phosphate, whereas IMPA2 shows significantly lower affinity
-
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
show the reaction diagram
Q57573
-
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
show the reaction diagram
Q57573
-
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
show the reaction diagram
Archaeoglobus fulgidus, Thermotoga maritima, Thermotoga maritima TM1415, Archaeoglobus fulgidus AF2372
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
D-alpha-galactose 1-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-alpha-glucose 1-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-beta glucose 1-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-erythrose 4-phosphate + H2O
D-erythrose + phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Q57573
very effective substrate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Q57573
very effective substrate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
-
very effective substrate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Methanocaldococcus jannaschii MJ0109
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Thermotoga maritima TM1415, Archaeoglobus fulgidus AF2372
-
very effective substrate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Archaeoglobus fulgidus AF2372
-
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Q57573
16% of the rate with inositol 1-phosphate
-
?
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Q57573
16% of the rate with inositol 1-phosphate
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-glucitol-6-phosphate + H2O
D-glucitol + phosphate
show the reaction diagram
-
hydrolyzed very slowly
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-mannitol-6-phosphate + H2O
D-mannitol + phosphate
show the reaction diagram
-
hydrolyzed very slowly
-
-
?
D-mannose 6-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1,2,3,4,5,6-hexakisphosphate + H2O
D-myo-inositol 1,2,3,4,5-pentakisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
O30298
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
B3DFH0, -
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-, P0ADG4
preferred substrate
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
catalytic mechanism and substrate-enzyme interactions
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
substrate binding structure, interactions sites with the enzyme involving Tyr155 and Ala172
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
O14732, P29218
IMPA1 shows strong activity towards D-myo-inositol 1-phosphate, whereas IMPA2 shows significantly lower affinity
-
-
?
D-myo-inositol 2-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-myo-inositol 3-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-xylose 5-phosphate + H2O
D-xylose + phosphate
show the reaction diagram
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
show the reaction diagram
B3DFH0, -
-
-
-
?
fructose 1-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
fructose 6-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
glucitol 6-phosphate + H2O
glucitol + phosphate
show the reaction diagram
-
-
-
?
glucose 1-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
glucose 1-phosphate + H2O
?
show the reaction diagram
-
high rate of hydrolysis
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
Q57573
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
Q57573
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
O33832
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
64% of the rate with inositol 1-phosphate
-
?
inosine 5'-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, ATCC 25618
-
-
-
-
?
inositol 4-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
the inositol ring docks to the enzyme by forming four hydrogen bonds: the 2-OH group with Asp104, the 3-OH with Asp231, the 5-OH group with Thr106, and the 6-OH with the carbonyl group of main chain of Gly205
-
-
?
L-chiro-inositol-3-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
L-chiro-inositol-3-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
L-glycerol 1-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
L-glycerol 1-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
L-glycerol 1-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
L-glycerol 1-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
-
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
show the reaction diagram
O30298
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
show the reaction diagram
O33832
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
show the reaction diagram
B3DFH0, -
-
-
-
-
myo-inositol 1,3-thiophosphate + H2O
?
show the reaction diagram
-
reaction 3times slower than reaction with inositol 1-phosphate
-
?
myo-inositol 1,4-bisphosphate + H2O
?
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Q57573
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Q57573
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
inversion of phosphate configuration
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
acts on D- and L-isomer
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
D- and L-isomer serve as substrate
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
D- and L-isomer, 2.5-fold higher activity with D-isomer
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
de novo biosynthesis of inositol precursor of inositol phospholipids
-
-
-
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
de novo biosynthesis of inositol, involved in phosphoinositide signaling pathway
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Q57573
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
show the reaction diagram
-
feed-back inhibition of inositol 1,4,5-triphosphate phosphate production by inositol monophosphates, involved in cell response to ammonium
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
involved in phosphatidylinositol signaling pathway
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
key metabolic step, de novo synthesis of myo-inositol, phosphatidylinositol is essential of growth
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Q57573
organism do not contain lipids with inositol head group, involved in the response to thermal stress
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
organism do not contain lipids with inositol head group, involved in the response to thermal stress
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
reguglation of exopolysaccharide synthesis suggested
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
regulation of phosphatidylinositol signaling pathway
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
synthesis of myo-inositol, that is a key substrate for synthesis of phosphatidylinositol
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
very low concentration of inositol compounds
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Methanocaldococcus jannaschii MJ0109
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Mycobacterium smegmatis MC2 155
-
-, key metabolic step, de novo synthesis of myo-inositol, phosphatidylinositol is essential of growth
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Mycobacterium tuberculosis H37Rv, ATCC 25618
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Thermotoga maritima TM1415, Archaeoglobus fulgidus AF2372
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Archaeoglobus fulgidus AF2372
-
-
-
?
myo-inositol 2-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 2-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
myo-inositol 2-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Q57573
15% of the rate with inositol 1-phosphate
-
?
myo-inositol 2-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Q57573
15% of the rate with inositol 1-phosphate
-
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Q6NPM8, Q94F00, Q9M8S8
-
-
-
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
inversion of phosphate configuration
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
the substrate shows a similar binding structure as inositol 5-phosphate
-
-
?
myo-inositol 4-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 4-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 5-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-, myo-inositol 5-phosphate forms an electrostatic interaction between the metal ions and phosphate moiety, and the 2-OH group forms a hydrogen bond with the carbonyl group of Gln224, the 3-OH with the nitrogen atom of side chain of Gln224, and 4-OH with Asp231. The non-bridging oxygen O9 interacts with the 4-OH group, and the bridging oxygen O1 with Mg2+-2
-
-
?
myo-inositol 6-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-, the substrate shows a similar binding structure as inositol 5-phosphate
-
-
?
myo-inositol phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
the reaction is only catalyzed in the presence of ZnCl2 at acidic pH
-
-
?
propan-1-ol 2-phosphate + H2O
1-propanol + phosphate
show the reaction diagram
-
-
-
-
?
purine nucleotides + H2O
?
show the reaction diagram
-
-
-
-
?
pyrimidine ribonucleotides + H2O
?
show the reaction diagram
-
-
-
-
?
scyllo-inositol 1-phosphate + H2O
scyllo-inositol + phosphate
show the reaction diagram
O14732, P29218
IMPA1 shows strong activity towards scyllo-inositol 1-phosphate, whereas IMPA2 shows almost no affinity
-
-
?
mannitol 1-phosphate + H2O
mannitol + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
avian and plant enzyme attack myo-inositol 2-phosphate, mammalian enzyme not
-
-
-
additional information
?
-
-
not: inorganic phosphate, myo-inositol pentaphosphate
-
-
-
additional information
?
-
-
small activity: 5-ribonucleotides
-
-
-
additional information
?
-
-
triphosphoinositide
-
-
-
additional information
?
-
-
not: inositol 2-phosphate, inositol 1,4-bisphosphate, inositol 1,4,5-triphosphate
-
-
-
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
-
?
additional information
?
-
Q57573
D-glucose 6-phosphate, D-fructose 6-phosphate, 5'-AMP and NAD+ are not hydrolyzed
-
?
additional information
?
-
Q57573
D-glucose 6-phosphate, D-fructose 6-phosphate, 5'-AMP and NAD+ are not hydrolyzed
-
?
additional information
?
-
-
no activity with 4-nitrophenyl phosphate, 5'-AMP, NAD+, glucose 1-phosphate and glucose 6-phosphate
-
?
additional information
?
-
-
no activity with glucose 6-phosphate and 5'-AMP
-
?
additional information
?
-
-
traces of activity with glucose 1-phosphate and 4-nitrophenylphosphate, no activity with glucose 6-phosphate and 5'-AMP
-
?
additional information
?
-
-
traces of activity with glucose 1-phosphate, no activity with 4-nitrophenyl phosphate and fructose 1,6-bisphosphate
-
?
additional information
?
-
-, O30298
at temperatures above 80C 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
?
-
-
key enzyme in the phosphoinositide cell-signaling system
-
-
-
additional information
?
-
-
the enzyme is involved in development of bipolar disorder
-
-
-
additional information
?
-
P20456
the enzyme is the key enzyme of the phosphatidylinositol signalling pathway and the putative target of the mood-stabilizing drug lithium
-
-
-
additional information
?
-
-
the organism does not accumulate di-myo-inositol 1,1'-phosphate at temperatures above 80C
-
-
-
additional information
?
-
-
substrate specificity, enzyme is both inositol monophosphatase and fructose-1,6-bisphosphatase
-
-
-
additional information
?
-
-, O30298
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
?
-
-
does not hydrolyze p-nitrophenyl phosphate, ADP, AMP or D-glucose 6-phosphate
-
-
-
additional information
?
-
-
the enyzme 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
?
-
-
substrate binding structure of IMPA2, docking study on other myo-inositol monophosphates, overview. Common binding patterns: the non-bridging oxygen atom O9 coordinated Mg2+-3 and O8 coordinated both Mg2+-1 and Mg2+-2. The bridging oxygen atom coordinated Mg2+-2. No activity with inositol 2-phosphate
-
-
-
additional information
?
-
Thermotoga maritima TM1415, Archaeoglobus fulgidus AF2372
-
archeal enzyme displays inositol monophosphatase as well as fructose 1,6-bisphosphatase activity
-
?
additional information
?
-
Archaeoglobus fulgidus AF2372
-
archeal enzyme displays inositol monophosphatase as well as fructose 1,6-bisphosphatase activity
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Q57573
very effective substrate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
Archaeoglobus fulgidus, Thermotoga maritima, Thermotoga maritima TM1415, Archaeoglobus fulgidus AF2372
-
very effective substrate
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-, O30298
-
-
-
?
inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, ATCC 25618
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
-
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
de novo biosynthesis of inositol precursor of inositol phospholipids
-
-
-
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
de novo biosynthesis of inositol, involved in phosphoinositide signaling pathway
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Q57573
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
show the reaction diagram
-
feed-back inhibition of inositol 1,4,5-triphosphate phosphate production by inositol monophosphates, involved in cell response to ammonium
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
involved in phosphatidylinositol signaling pathway
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
key metabolic step, de novo synthesis of myo-inositol, phosphatidylinositol is essential of growth
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Q57573
organism do not contain lipids with inositol head group, involved in the response to thermal stress
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
organism do not contain lipids with inositol head group, involved in the response to thermal stress
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
reguglation of exopolysaccharide synthesis suggested
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
regulation of phosphatidylinositol signaling pathway
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
synthesis of myo-inositol, that is a key substrate for synthesis of phosphatidylinositol
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
very low concentration of inositol compounds
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Methanocaldococcus jannaschii MJ0109
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Mycobacterium smegmatis MC2 155
-
key metabolic step, de novo synthesis of myo-inositol, phosphatidylinositol is essential of growth
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Archaeoglobus fulgidus AF2372
-
-
-
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
Q6NPM8, Q94F00, Q9M8S8
-
-
-
?
myo-inositol 4-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 5-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
myo-inositol 6-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
show the reaction diagram
-, O30298
-
-
-
?
additional information
?
-
-, O30298
at temperatures above 80C 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
?
-
-
key enzyme in the phosphoinositide cell-signaling system
-
-
-
additional information
?
-
-
the enzyme is involved in development of bipolar disorder
-
-
-
additional information
?
-
P20456
the enzyme is the key enzyme of the phosphatidylinositol signalling pathway and the putative target of the mood-stabilizing drug lithium
-
-
-
additional information
?
-
-
the organism does not accumulate di-myo-inositol 1,1'-phosphate at temperatures above 80C
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
3% activation at 3.5 mM
Ca2+
-
no activity at 3 mM
Ca2+
Q57573
two ions bound per subunit
Ca2+
-
activates
Ca2+
-
required
Co2+
-
40% stimulation; less effective than Mg2+, cannot substitute for Mg2+
Co2+
-
less effective than Mg2+, cannot substitute for Mg2+
Co2+
-
3% activation at 3.5 mM
Co2+
-
-
Co2+
-
partial activation of enzyme, 16.8% of the activity observed with Mg2+
Co2+
-
partial activation
Co2+
-
30% of the activity with Mg2+
Co2+
-
activates
Cu2+
-
3% activation at 3.5 mM
Cu2+
-
slight activation
Cu2+
-
activates
Fe2+
-
less effective than Mg2+, cannot substitute for Mg2+
Fe2+
-
less effective than Mg2+, cannot substitute for Mg2+
Fe2+
-
3% activation at 3.5 mM
Fe2+
-
slight activation
Fe2+
-
very weak activation
Fe2+
-
30% of the activity with Mg2+
KCl
-
in its absence activation by Mg2+ occurres at 2fold lower concentrations
Li+
-
at 100 mM the activity is slightly enhanced
Li+
-
very potent inhibitor
Li+
-
127% activity in the presence of 500 mM Li+
Li+
-
activates only in the presence of Mg2+
Mg2+
-
dependent on
Mg2+
-
stimulates
Mg2+
-
dependent on
Mg2+
-
dependent on
Mg2+
-
completely dependent on
Mg2+
-
dependent on
Mg2+
-
dependent on
Mg2+
-
duodenal IMPase is less dependent on Mg2+ than the brain one
Mg2+
-
-
Mg2+
-
required, highest activity with 3 mM Mg2+, inhibitory at high concentrations, 50% inhibition at 100 mM
Mg2+
-
required, highest activity at 6 mM Mg2+, inhibitory at higher concentrations
Mg2+
-
required, highest activity with 6 mM Mg2+
Mg2+
-
required, highest activity 6-100 mM Mg2+, inhibitory above 100 mM
Mg2+
-
two molecules bound per subunit
Mg2+
P20456
dependent on, three Mg2+ are octahedrally coordinated at the active site of each of the two subunits involving residues E70, D90, I92, D93, and D220, detailed three-metal mechanism, overview
Mg2+
-
dependent on
Mg2+
-
dependent on, involved in temeprature-dependent substrate affinity regulation
Mg2+
-
required, 2 Mg2+ per active site, involved in catalysis
Mg2+
-
activates
Mg2+
O14732, P29218
required; required
Mg2+
-
cofactor requirement for 3 Mg2+ ions
Mg2+
-
optimal activation effect at 3 mM
Mg2+
-
required for catalytic activity, the phosphate moiety coordinates three Mg2+ ions, and the inositol ring forms hydrogen bonds with the amino acids conserved in the family. 3D models of three- and two-Mg2+-ion bound myo-inositol monophosphatase 2, docking and binding structure analysis, 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
Mn2+
-
stimulates slightly
Mn2+
-
stimulates
Mn2+
-
3% activation at 3.5 mM
Mn2+
-
stimulates
Mn2+
-
gave 17% of the acitivity provided with Mg2+; stimulates
Mn2+
-
partial activation of enzyme, 22.7% of the activity observed with Mg2+
Mn2+
-
partial activation
Mn2+
Q57573
three ions bound per subunit
Mn2+
-
13% of the activity with Mn2+
Na+
-
-
NH4+
-
stimulatory
NH4+
-
stimulatory
Ni2+
-
partial activation
Zn2+
-
40% stimulation
Zn2+
-
less effective than Mg2+
Zn2+
-
activation at 3.5 mM
Zn2+
-
partial activation of enzyme, 8.2% of the activity observed with Mg2+
Zn2+
-
no effect between 0.01-10 mM
Zn2+
-
very weak activation
Zn2+
Q57573
three ions bound per subunit
Mn2+
-
can partially substitute for Mg2+
additional information
-
absolute requirement for divalent cations, Mg2+ greatest activity
additional information
-
no activity wth Co2+, Ni2+, Cu2+, Zn2+, and Ca2+, no effect by Na+ and K+
additional information
O14732, P29218
the enzyme shows weaker or almost no activity when Mg2+ is replaced by Ca2+, Mn2+, Na+, or K+ (2 mM each); the enzyme shows weaker or almost no activity when Mg2+ is replaced by Ca2+, Mn2+, Na+, or K+ (2 mM each)
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
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl 1-methylphosphonate
-
IC50 is 260 mM
(-)-(1R,2R,4R,6R)-6-propyloxy-2,4-dihydroxycyclohexyl 1-ethylphosphonate
-
competitive inhibition
(-)-(1R,2R,4R,6R)-6-propyloxy-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
competitive inhibition
(-)-(1S,2R,4R,6R)-6-propyloxycyclohexane-1,2,4-triol
-
IC50 is about 150 mM
(-)-(1S,2R,4S,6R)-6-(2-aminoethyloxy)cyclohexane-1,2,4-triol
-
IC50 is 5 mM
(-)-(1S,2R,4S,6R)-6-(2-phenylethyl)amino-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
IC50 is above 54 mM
(-)-(1S,2R,4S,6R)-6-(2-phenylethyl)aminocyclohexane-1,2,4-triol
-
IC50 is 6 mM
(-)-(1S,2R,4S,6R)-6-(3-aminopropyloxy)cyclohexane-1,2,4-triol
-
IC50 is 10 mM
(-)-(1S,2R,4S,6R)-6-(4-phenylbutyl)aminocyclohexane-1,2,4-triol
-
non-competitive inhibition
(-)-(1S,2R,4S,6R)-6-aminocyclohexane-1,2,4-triol
-
IC50 is above 50 mM
(-)-(1S,2R,4S,6R)-6-butylaminocyclohexane-1,2,4-triol
-
non-competitive inhibition in absence of phosphate
(-)-(1S,2R,4S,6R)-6-ethylaminocyclohexane-1,2,4-triol
-
IC50 is above 50 mM
(-)-(1S,2R,4S,6R)-6-hexylamino-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
IC50 is 1.3 mM
(-)-(1S,2R,4S,6R)-6-hexylaminocyclohexane-1,2,4-triol
-
uncompetitive inhibition
(-)-(1S,2R,4S,6R)-6-hexyloxycyclohexane-1,2,4-triol
-
IC50 is about 10 mM
(-)-(1S,2R,4S,6R)-6-methylamino-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
IC50 is above 8 mM
(-)-(1S,2R,4S,6R)-6-octylaminocyclohexane-1,2,4-triol
-
IC50 is 4 mM
(-)-(1S,2R,4S,6R)-6-[4-(2-hydroxyphenyloxy)butyloxy]cyclohexane-1,2,4-triol
-
competitive inhibition
(-)-(1S,2R,4S,6R)-6-[N-(4-phenylbutyl)-N-(2-aminoethyl)-amino]cyclohexane-1,2,4-triol [hydrochloride salt]
-
IC50 is 9 mM
(1R,2R,4R,6R)-2,4-dihydroxy-6-[4-(2-hydroxyphenyl)butoxy]cyclohexyl phosphate
-
-
(1S,2R,4S,6R)-6-(butylamino)cyclohexane-1,2,4-triol
-
-
(NH4)2SO4
-
30% inhibition at 10 mM
(phenylmethanediyl)bis(phosphonic acid)
-
-
1-(4-hydroxyphenyloxy)ethane-1,1-bisphosphonic acid
-
L-690,330
-
1-(4-hydroxyphenyloxy)ethane-1,1-bisphosphonic acid
-
-
-
2,3,7-trihydroxycyclohepta-2,4,6-trien-1-one
-
-
2-deoxyglucose-6-phosphate
-
-
2-mercaptoethanol
-
-
3-phosphoglycerate
-
weak competetive inhibitor
6-phosphogluconate
-
slight
acetonitrile
-
-
Be2+
-
50% inhibition at 0.09 mM
Ca2+
-
Ca2+/EGTA buffer, not: 0.0001-0.01 mM
Ca2+
-
strong competitive against Mg2+
Ca2+
-
inhibits only at millimolar concentrations
Ca2+
-
50% inhibition at 0.4 mM
Carbachol
-
in combination with Li
Co2+
-
inhibits hydrolysis of inositol-1-phosphate at high concentrations
Co2+
-
50% inhibition at 0.7 mM
Cr2+
-
50% inhibition at 3 mM
Cu2+
-
50% inhibition at 1 mM
Dimethylsulfoxide
-
5% inhibition
Disulfiram
-
-
dithiothreitol
-
-
DL-myo-inositol 1-phosphate
B3DFH0, -
-
F-
-
50% inhibitory at 1 mM
Heavy metal ions
-
-
-
HgCl2
-
95% inhibition at 1 mM
iodoacetate
-
30% inhibition at 10 mM
L-690330
-
bisphosphonate enzyme inhibitor
L-690488
-
a tetrapivaloyloxymethyl ester prodrug of L-690330
Li+
-
inhibits 50% of activity at 1 mM, uncompetitive inhibitor
Li+
-
substantial inhibition at 250 mM
Li+
-
250 mM inhibits about 65%, 1000 mM about 90%
Li+
-
inhibits at millimolar concentrations
Li+
-
different Li-isotopes do not possess differential lethality effects in vivo
Li+
-
50% inhibitory at 100 mM
Li+
-
1.25 mM is 50% inhibitory
Li+
-
at 100 mM 72% inhibition of the brain enzyme but only 27% of the duodenal enzyme
Li+
-
50% inhibition at 0.8 mM, also able to inhibit cell growth
Li+
Q57573
poor inhibition
Li+
-
50% inhibition at 0.9 mM
Li+
P20456
binding structure, modelling of the lithium-inhibited enzyme-product complex
Li+
-
inhibitory, but can amplify the effect of Mg2+
Li+
O14732, P29218
;
Li+
B3DFH0, -
0-4 mM LiCl, 3 mM Li+ inhibits activity by approximately 50%, inhibition increases with Li+ concentration
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
Mg2+
-
inhibits hydrolysis of inositol-1-phosphate at high concentrations
Mg2+
-
slight inhibition at 100 mM
Mg2+
-
tight binding of Mg2+ to the protein affects the secondary structure
Mn2+
-
strong competitive against Mg2+
Mn2+
-
inhibits only at millimolar concentrations
Mn2+
-
50% inhibition at 0.8 mM
myo-Inositol
-
product inhibition, competitive
myo-Inositol
-
non-competitive inhibition
myo-inositol 1,3,4,5,6 pentakis(dihydrogen phosphate)
-
-
myo-Inositol tetrakis(dihydrogen phosphate)
-
-
N-ethylmaleimide
-
substrate and Mg2+ protect
Na+
-
50% inhibition at 70 mM
Na2MoO4
-
30% inhibition at 10 mM
NaF
-
inhibits by 60% and 100% at 1 mM and 5 mM respectively
NaF
-
45% inhibition at 1 mM
NaF
-
90% inhibition by 10 mM
Ni2+
-
50% inhibition at 30 mM
O2
-
activity of the native enzyme but not the C150S mutant can be completely abolished with oxygen, reversible with thiol-containing compounds
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Phenylmercuric nitrate
-
-
phosphate
-
-
phosphate
-
product inhibition, competitive
phosphate
-
product inhibition, competitive
phosphosulfate
-
-
pyridoxal-5'-phosphate
-
inactivates the enzyme by covalent binding to the lysine residue of a specific binding site LQVSQQEDITK at or near the substrate binding site, the substrate D-myo-inositol 1-phosphate protects against the inactivation
Ribose-5-phosphate
-
-
SO42-
-
hydrolyzed very slowly
SO42-
-
40% inhibitory at 17 mM
sulfhydryl reagents
-
-
sulfhydryl reagents
-
-
thioredoxin
-
inhibits native enzyme but nut C150S mutant
Zn2+
-
50% inhibition at 0.005 mM
monoclonal antibody [DV1]
-
one of five antibodies was found to inhibit the enzyme activity
-
additional information
-
Li+, glycerol and glucose in the culture medium depresses enzyme expression, no inhibition with valproate
-
additional information
-
high-throughput cell-based screening using scintillation proximity assay measuring G-protein-coupled receptor activation for evaluation of inhibitory potency of lithium mimetics, overview
-
additional information
-
potency and structural features of product-like inhibitors, inhibitory mechanism, overview
-
additional information
-
not inhibited by butanedione monoxime, or orthovanadate
-
additional information
-
Na+, K+, NH4+ have no significant effect on the enzyme activity
-
additional information
-
300 mM Na+ or K+have no effect
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
calbindin
-
apo and Ca2+-bound form, strong activation, Kd: approximately 0.001 mM, at pH 6 very low activity in the absence of calbindin, almost no activity lost in the presence of calbindin compared to activity at pH 7
-
NH4+
-
stimulatory
NH4+
-
stimulatory
Mn2+
-, P0ADG4
activating
additional information
-
expression is increased in the presence of inositol
-
additional information
-
the enzyme is not upregulated upon thermal stress
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.025
-
(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl-1-hydroxyphosphonate cyclohexylammonium salt
-
pH 8.0, 25C
0.044
-
1-L-chiro-inositol-3-phosphate
-
-
0.083
-
2'-AMP
-
-
0.17
-
2'-AMP
-
-
0.19
-
2'-AMP
-
-
0.58
-
2'-AMP
-
-
1.58
-
2'-AMP
-
-
0.09
-
2'-GMP
-
-
0.372
-
3'-AMP
-
-
0.051
-
3,5-dideoxy-D-myo-inositol 1-phosphate
-
pH 8.0, 37C
0.16
-
3,5-dideoxy-D-myo-inositol 1-phosphate
-
pH 8.0, 85C
0.1
-
3,5-dideoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 37C
4.9
-
3,5-dideoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 85C
0.047
-
3-deoxy-D-myo-inositol 1-phosphate
-
pH 8.0, 37C
0.23
-
3-deoxy-D-myo-inositol 1-phosphate
-
pH 8.0, 85C
0.2
-
3-deoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 37C
2.3
-
3-deoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 85C
3.8
-
4-nitrophenyl phosphate
-
native enzyme, pH 8.0, 80C
4.1
-
4-nitrophenyl phosphate
-
C150S mutant enzyme, pH 8.0, 80C
5
-
4-nitrophenyl phosphate
-
-
0.038
-
D-fructose 1,6-bisphosphate
Q57573
85C
2
-
D-glucitol-6-phosphate
-
-
0.078
-
D-inositol 1-phosphate
-
-
0.13
-
D-inositol 1-phosphate
-
-
0.12
-
D-inositol-1-phosphate
-
-
0.148
-
D-inositol-1-phosphte
-
-
0.82
-
D-mannitol-6-phosphate
-
-
0.06
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme V249A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.068
-
D-myo-Inositol 1-phosphate
-
pH 8.0, 37C
0.1
-
D-myo-Inositol 1-phosphate
-
pH 8.0, 25C
0.11
-
D-myo-Inositol 1-phosphate
-
pH 8.0, 85C
0.11
-
D-myo-Inositol 1-phosphate
-, P0ADG4
wild type enzyme, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.13
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme R121A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C; mutant enzyme R248A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.16
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme R183A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.17
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme H98F, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.18
-
D-myo-Inositol 1-phosphate
-
-
0.22
-
D-myo-Inositol 1-phosphate
-
pH 9.3, 37C, recombinant wild-type enzyme
0.29
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme R184A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
1.02
-
D-myo-Inositol 1-phosphate
-
-
0.061
-
D-myo-inositol 3-phosphate
-
pH 8.0, 37C
1.7
-
D-myo-inositol 3-phosphate
-
pH 8.0, 85C
0.0034
-
DL-myo-inositol 1-phosphate
-
in the presence of 3 mM MgCl2 in 50 mM Tris-Cl (pH 8), at 42C
0.0097
-
DL-myo-inositol 1-phosphate
B3DFH0, -
recombinant protein, 9.7 microM substrate, higher affinity as compared with reported Km values for other eukaryotic IMPases
0.082
-
DL-myo-inositol 1-phosphate
-
-
0.086
-
DL-myo-inositol 1-phosphate
-
-
0.09
-
DL-myo-inositol 1-phosphate
-
brain IMPase
0.12
-
DL-myo-inositol 1-phosphate
-
-
0.12
-
DL-myo-inositol 1-phosphate
-
-
0.145
-
DL-myo-inositol 1-phosphate
-
-
0.15
-
DL-myo-inositol 1-phosphate
-
duodenal IMPase
0.46
-
DL-myo-inositol 1-phosphate
-
measured in human serum
0.57
-
DL-myo-inositol 1-phosphate
-
-
0.89
-
DL-myo-inositol 1-phosphate
-
-
1.67
-
DL-myo-inositol 1-phosphate
-
-
1.71
-
glucose-6-phosphate
-
-
0.061
-
Glycerol 2-phosphate
-
-
0.2
-
Glycerol 2-phosphate
-
duodenal IMPase
0.34
-
Glycerol 2-phosphate
-
brain IMPase
0.38
-
Glycerol 2-phosphate
-
-
0.77
-
Glycerol 2-phosphate
-
-
4.17
-
Glycerol 2-phosphate
-
-
0.21
-
inositol 1,3-thiophosphate
-
pH 9.0, 25C
0.286
-
inositol 2-phosphate
-
-
0.733
-
inositol 2-phosphate
-
-
0.11
-
inositol 3-phosphate
-
pH 9.0, 25C
0.35
-
inositol-2-phosphate
-
-
0.382
-
L-glycerol 1-phosphate
-
-
0.562
-
L-glycerol 1-phosphate
-
-
0.87
-
L-glycerol 1-phosphate
-
-
0.079
-
L-inositol 1-phosphate
-
pH 8.0, 37C
0.061
-
L-myo-Inositol 1-phosphate
-
pH 8.0, 37C
0.082
-
L-myo-Inositol 1-phosphate
-
-
0.1
-
L-myo-Inositol 1-phosphate
-
-
0.8
-
L-myo-Inositol 1-phosphate
-
-
1.67
-
L-myo-Inositol 1-phosphate
-
85C
1.7
-
L-myo-Inositol 1-phosphate
-
pH 8.0, 85C
13.2
-
L-myo-Inositol 1-phosphate
-
75C
0.12
-
L-myo-inositol-1-phosphate
-
-
0.064
-
myo-inositol 1-phosphate
-
pH 8.0, 37C
0.07
-
myo-inositol 1-phosphate
-
37C
0.091
-
myo-inositol 1-phosphate
Q57573
85C
0.11
-
myo-inositol 1-phosphate
-
85C
0.13
-
myo-inositol 1-phosphate
-
95C
0.177
-
myo-inositol 1-phosphate
-
pH 8.5, 37C
0.23
-
myo-inositol 1-phosphate
-
pH 7.8, 30C
66
-
myo-inositol 1-phosphate
-
pH 7.5, 37C
15
-
Propan-1-ol 2-phosphate
-
-
0.235
-
Sodium diphosphate
-
at 37C, in 25 mM phosphate buffer with 2 mM dithiothreitol (pH 7.0) and 2 mM MgCl2
3.2
-
Mg2+
-
pH 7.5, 37C
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 55C and 70C, but fructose bisphosphate is not stable above 70C
-
additional information
-
additional information
-
analysis of temperature-dependence of the Km value of inositol 1-phosphate substrates, kinetic analysis
-
additional information
-
additional information
-
reaction kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.49
-
3,5-dideoxy-D-myo-inositol 1-phosphate
-
pH 8.0, 85C
2.5
-
3,5-dideoxy-D-myo-inositol 1-phosphate
-
pH 8.0, 85C
4.4
-
3,5-dideoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 37C
5.78
-
3,5-dideoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 85C
5.8
-
3,5-dideoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 85C
3.9
-
3-deoxy-D-myo-inositol 1-phosphate
-
pH 8.0, 85C
4.4
-
3-deoxy-D-myo-inositol 1-phosphate
-
pH 8.0, 37C
3.2
-
3-deoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 85C
5.6
-
3-deoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 37C
2.7
-
D-fructose 1,6-bisphosphate
-
85C
2.7
-
D-fructose 1,6-bisphosphate
Q57573
50C
7
-
D-fructose 1,6-bisphosphate
Q57573
85C
268
-
D-fructose 1,6-bisphosphate
-
95C
0.165
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme K251A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.175
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme V249A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.199
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme R199A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.267
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme R248A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.357
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme R184I, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.369
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme R121A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.49
-
D-myo-Inositol 1-phosphate
-, P0ADG4
wild type enzyme, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.504
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme H98F, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
0.747
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme R183A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
1.183
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme R184A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
3.3
-
D-myo-Inositol 1-phosphate
-
pH 8.0, 85C
4.1
-
D-myo-Inositol 1-phosphate
-
-
4.32
-
D-myo-Inositol 1-phosphate
-
pH 8.0, 85C
4.4
-
D-myo-Inositol 1-phosphate
-
pH 8.0, 37C
6.08
-
D-myo-Inositol 1-phosphate
-, P0ADG4
mutant enzyme H98F, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C; mutant enzyme R183A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C; mutant enzyme R184A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37C
7.72
-
D-myo-Inositol 1-phosphate
-
pH 8.0, 85C
28.7
-
D-myo-Inositol 1-phosphate
-
-
104
-
D-myo-Inositol 1-phosphate
-
pH 8.0, 85C
1.4
-
D-myo-inositol 3-phosphate
-
pH 8.0, 37C
3.6
-
D-myo-inositol 3-phosphate
-
pH 8.0, 85C
1.29
-
DL-myo-inositol 1-phosphate
B3DFH0, -
recombinant protein
0.19
-
inositol 1,3-thiophosphate
-
pH 9.0, 25C
0.48
-
inositol 3-phosphate
-
pH 9.0, 25C
1.4
-
L-myo-Inositol 1-phosphate
-
pH 8.0, 37C
3.6
-
L-myo-Inositol 1-phosphate
-
pH 8.0, 85C
3.64
-
L-myo-Inositol 1-phosphate
-
pH 8.0, 85C
7.92
-
L-myo-Inositol 1-phosphate
-
pH 8.0, 85C
1.5
-
myo-inositol 1-phosphate
Q57573
50C
2.5
-
myo-inositol 1-phosphate
-
85C
3.6
-
myo-inositol 1-phosphate
-
pH 8.5, 37C
4.2
-
myo-inositol 1-phosphate
Q57573
85C
6.5
-
myo-inositol 1-phosphate
-
37C
207
-
myo-inositol 1-phosphate
-
95C
4
-
3,5-dideoxy-D-myo-inositol 1-phosphate
-
pH 8.0, 37C
additional information
-
3,5-dideoxy-L-myo-inositol 1-phosphate
-
pH 8.0, 85C
16.6
-
L-myo-Inositol 1-phosphate
-
pH 8.0, 85C
additional information
-
additional information
-
values extrapolated from Arrhenius plot
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.16
-
(-)-(1R,2R,4R,6R)-6-propyloxy-2,4-dihydroxycyclohexyl 1-ethylphosphonate
-
pH 8.0, 25C
0.04
-
(-)-(1R,2R,4R,6R)-6-propyloxy-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
pH 8.0, 25C
9
-
(-)-(1S,2R,4S,6R)-6-(4-phenylbutyl)aminocyclohexane-1,2,4-triol
-
pH 8.0, 25C
0.3
-
(-)-(1S,2R,4S,6R)-6-butylaminocyclohexane-1,2,4-triol
-
pH 8.0, 25C
0.3
-
(-)-(1S,2R,4S,6R)-6-hexylaminocyclohexane-1,2,4-triol
-
pH 8.0, 25C
4
-
(-)-(1S,2R,4S,6R)-6-[4-(2-hydroxyphenyloxy)butyloxy]cyclohexane-1,2,4-triol
-
pH 8.0, 25C
0.3
-
(1S,2R,4S,6R)-6-(butylamino)cyclohexane-1,2,4-triol
-
-
3.84
-
DL-myo-inositol 1-phosphate
B3DFH0, -
recombinant protein
4.35
-
Li+
-
pH 7.8, 30C
39
-
myo-Inositol
-
pH 7.5, 37C
2.7
-
phosphate
-
pH 7.5, 37C
0.5
-
phosphosulfate
-
pH 6.5 and pH 9.0
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
260
-
(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl 1-methylphosphonate
-
IC50 is 260 mM
150
-
(-)-(1S,2R,4R,6R)-6-propyloxycyclohexane-1,2,4-triol
-
IC50 is about 150 mM
5
-
(-)-(1S,2R,4S,6R)-6-(2-aminoethyloxy)cyclohexane-1,2,4-triol
-
IC50 is 5 mM
54
-
(-)-(1S,2R,4S,6R)-6-(2-phenylethyl)amino-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
IC50 is above 54 mM
6
-
(-)-(1S,2R,4S,6R)-6-(2-phenylethyl)aminocyclohexane-1,2,4-triol
-
IC50 is 6 mM
10
-
(-)-(1S,2R,4S,6R)-6-(3-aminopropyloxy)cyclohexane-1,2,4-triol
-
IC50 is 10 mM
50
-
(-)-(1S,2R,4S,6R)-6-aminocyclohexane-1,2,4-triol
-
IC50 is above 50 mM
50
-
(-)-(1S,2R,4S,6R)-6-ethylaminocyclohexane-1,2,4-triol
-
IC50 is above 50 mM
1.3
-
(-)-(1S,2R,4S,6R)-6-hexylamino-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
IC50 is 1.3 mM
10
-
(-)-(1S,2R,4S,6R)-6-hexyloxycyclohexane-1,2,4-triol
-
IC50 is about 10 mM
8
-
(-)-(1S,2R,4S,6R)-6-methylamino-2,4-dihydroxycyclohexyl 1-methylphosphonate
-
IC50 is above 8 mM
4
-
(-)-(1S,2R,4S,6R)-6-octylaminocyclohexane-1,2,4-triol
-
IC50 is 4 mM
9
-
(-)-(1S,2R,4S,6R)-6-[N-(4-phenylbutyl)-N-(2-aminoethyl)-amino]cyclohexane-1,2,4-triol [hydrochloride salt]
-
IC50 is 9 mM
0.00007
-
(1R,2R,4R,6R)-2,4-dihydroxy-6-[4-(2-hydroxyphenyl)butoxy]cyclohexyl phosphate
-
-
0.0002
-
(phenylmethanediyl)bis(phosphonic acid)
-
-
0.0002
-
1-(4-hydroxyphenyloxy)ethane-1,1-bisphosphonic acid
-
-
-
0.0008
-
2,3,7-trihydroxycyclohepta-2,4,6-trien-1-one
-
-
0.7
-
Li+
O14732, P29218
IMPA1, in the presence of 2 mM MgCl2
6
-
Li+
-
in the presence of 3 mM MgCl2 in 50 mM Tris-Cl (pH 8), at 42C
12
-
Li+
-
mutant D38A, pH not specified in the publication, 85C
25
-
Li+
O14732, P29218
IMPA2, in the presence of 2 mM MgCl2
240
-
Li+
-
wild-type enzyme, pH not specified in the publication, 85C
290
-
Li+
-
pH 8.0, 85C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.7
-
-
purified enzyme
3.3
-
-
purified enzyme, pH 8.0, 37C
4.37
-
-
total cell extract, at 37C, using sodium diphosphate supplemented with MgCl2 as a substrate
5
-
-
-
15
-
-
-
375.6
-
-
after 85.94fold purification, at 37C, using sodium diphosphate supplemented with MgCl2 as a substrate
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
when grown on glycerol highest activity at the end of exponential growth phase, when grown on glucose highest activity in the middle of exponential growth phase
additional information
-
-
scintillation proximity assay development
additional information
-
-
different assay methods, overview
additional information
-
B3DFH0, -
initial characterization of the genomic structure including promoter elements, expression of the single copy IMP-1 gene, expression levels not significantly altered by abiotic stress treatments, catalytic properties well suited for a role in myo-inositol synthesis
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
7.5
O14732, P29218
IMPA1
7
-
-
-
7
-
-
assay at
7.25
-
-
-
7.4
-
-
for L-myo-inositol-1-phosphate
7.4
-
-
-
7.4
-
-
-
7.4
-
-
assay at
7.5
8
-
-
7.5
8
O14732, P29218
IMPA2
8
-
-
for 2-AMP, beta-glycerophosphate
8
-
-
assay at
8
-
-
in 50 mM Tris-Cl buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
9
-
-
6.5
7.2
-
-
7
9
-
no significant changes in activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
37
-
-
-
37
-
-
assay at
37
-
-
assay at
37
-
-
-
42
-
-
optimally active at about 42C
85
-
-
or above
85
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
50
-
more than 30% and 50% of the maximal activity is reduced at 45C and 50C, respectively
55
85
-
the activity increases with increasing temperature, temperature profile
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.9
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
O14732, P29218
;
Manually annotated by BRENDA team
O14732, P29218
;
Manually annotated by BRENDA team
Q6NPM8, Q94F00, Q9M8S8
-
Manually annotated by BRENDA team
O14732, P29218
;
Manually annotated by BRENDA team
O14732, P29218
;
Manually annotated by BRENDA team
O14732, P29218
;
Manually annotated by BRENDA team
O14732, P29218
;
Manually annotated by BRENDA team
B3DFH0, -
4 week old plants
Manually annotated by BRENDA team
O14732, P29218
;
Manually annotated by BRENDA team
-
required in central interneurons of the mature nervous system for correct localization of synaptic components and thus for normal behavior
Manually annotated by BRENDA team
O14732, P29218
;
Manually annotated by BRENDA team
B3DFH0, -
4 week old plants
Manually annotated by BRENDA team
Q6NPM8, Q94F00, Q9M8S8
-
Manually annotated by BRENDA team
B3DFH0, -
early development stage, wild-type and mutant plants
Manually annotated by BRENDA team
Q6NPM8, Q94F00, Q9M8S8
-
Manually annotated by BRENDA team
O14732, P29218
;
Manually annotated by BRENDA team
Q6NPM8, Q94F00, Q9M8S8
flowering; flowering; flowering
Manually annotated by BRENDA team
O14732, P29218
;
Manually annotated by BRENDA team
additional information
Q6NPM8, Q94F00, Q9M8S8
the tissue-specific expression patterns of IMP and VTC4 genes, IMPL1 GUS expression is observed in all tissues, IMPL2 GUS expression is comparatively strong in roots, but has little hypocotyl expression. Expression of genes VTC4, IMPL1, and IMPL2 during plant development, quantitative PCR, overview; the tissue-specific expression patterns of IMP and VTC4 genes, IMPL1 GUS expression is observed in all tissues, IMPL2 GUS expression is comparatively strong in roots, but has little hypocotyl expression. Expression of genes VTC4, IMPL1, and IMPL2 during plant development, quantitative PCR, overview; the tissue-specific expression patterns of IMP and VTC4 genes, IMPL1 GUS expression is observed in all tissues, IMPL2 GUS expression is comparatively strong in roots, but has little hypocotyl expression. Expression of genes VTC4, IMPL1, and IMPL2 during plant development, quantitative PCR, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
O14732, P29218
;
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Staphylococcus aureus (strain MSSA476)
Staphylococcus aureus (strain MSSA476)
Staphylococcus aureus (strain MSSA476)
Staphylococcus aureus (strain MSSA476)
Staphylococcus aureus (strain MSSA476)
Staphylococcus aureus (strain MSSA476)
Staphylococcus aureus (strain MSSA476)
Staphylococcus aureus (strain MSSA476)
Staphylococcus aureus (strain MSSA476)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
11400
-
-
sucrose density sedimentation
28000
-
-
SDS-PAGE
29000
-
-
SDS-PAGE
29000
-
-
SDS-PAGE
29200
-
-
calculated from amino acid sequence
29920
-
-
ESI-MS
30000
-
-
calculated from amino acid sequence
30350
-
-
calculated mass of the Escherichia coli expressed protein
30500
-
-
gel filtration at low ionic strength
30510
-
-
analytical ultracentrifugation
31800
-
-
calculated from amino acid sequence
32000
-
-
SDS-PAGE
32000
-
-
SDS-PAGE
32000
-
-
SDS-PAGE, recombinant enzyme
37000
-
B3DFH0, -
SDS-PAGE
39000
-
-
gel filtration in the presence of 250 mM KCl
48000
-
-
gel filtration
54000
-
-
gel filtration
55000
-
-
gel filtration
55000
-
-
gel filtration
58000
-
-
gel filtration
58000
-
-
gel filtration
58000
-
-
gel filtration
59000
-
-
gel filtration
59000
-
-
gel filtration
59000
-
-
gel filtration
60000
-
-
gel filtration
60000
-
-
SDS-PAGE
62500
-
-
native PAGE, recombinant wild-type enzyme
64900
-
-
IMPA2, analytical ultracentrifugation
67000
-
-
gel filtration and gel eletrophoresis
70000
-
O14732, P29218
SDS-PAGE; SDS-PAGE
93000
-
-
native PAGE
116000
-
-
chromatography on bio-gel as well as gel electrophoresis
119000
-
-
gel filtration
210000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 30000, SDS-PAGE
?
-
western blot analysis
?
-
x * 43000, SDS-PAGE
?
-
x * 29000, SDS-PAGE and western blot analysis
?
B3DFH0, -
x * 37000, SDS-PAGE
?
-
x * 31000, about, sequence calculation
dimer
-
2 * 31000, SDS-PAGE
dimer
-
2 * 29000, SDS-PAGE
dimer
-
2 * 28000, SDS-PAGE
dimer
-
2 * 29000, SDS-PAGE
dimer
-
2 * 24000, SDS-PAGE
dimer
-
homodimer
dimer
-
crystal structure analysis
dimer
-
2 * 28000
dimer
P20456
structural comparison of subunits A and B, dimer interface structure, crystal structure, comparison to the structure of the human enzyme, overview
dimer
-
2 * 32000, about, recombinant wild-type enzyme, SDS-PAGE
dimer
-
2 * 30508, analytical ultracentrifugation, dimer in the presence of Mg2+ and in the crystal
dimer
-, P0ADG4
x-ray crystallography
dimer
-
in solution, analytical ultracentrifugation
dimer
-
2 * 32400, about, sequence calculation
dimer
Archaeoglobus fulgidus AF2372
-
; 2 * 28000
-
homodimer
O14732, P29218
x-ray crystallography; x-ray crystallography
homodimer
-
-
monomer
-
SDS-PAGE and gel filtration
monomer
-
-
tetramer
-
4 * 28000, SDS-PAGE
tetramer
-
4 * 52000, gel filtration after heating
tetramer
O33832
x-ray crystallography
tetramer
Thermotoga maritima TM1415
-
-
-
trimer
-
3 * 36000, SDs-PAGE
monomer
-
1 * 30508, analytical ultracentrifugation, SuhB is predominantly monomeric in the absence of the physiological activator Mg2+
additional information
-
comparative structural modeling, overview
additional information
-
IMPA2 structure analysis using IMPA1 crystal structure as a template, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
purified recombinant enzyme in complex with Mg2+, room temperature, hanging drop vapour diffusion method, 0.002 ml protein solution containing 20 mg/ml protein in 20 mm Tris-HCl, pH 7.5, and 20 mM MgCl2, is mixed with 0.002 ml reservoir solution containing 0.1 M sodium acetate, 0.1 M sodium HEPES, pH 8.5, and 15% PEG 4000, X-ray diffraction structure determination and analysis at 1.4 A resolution
P20456
the mutant protein R184A, which has equivalent IMPase activity to native SuhB, crystallizes under three different conditions: (1) 0.2 M ammonium iodide, 20% PEG 3350, pH6.2, (2) 0.2 M potassium acetate, 20% PEG 3350, pH 7.8, and (3) 0.2 M ammonium acetate, 20% PEG 3350, pH 7.1
-, P0ADG4
sitting drop vapour diffusion method, at 20C, with 10 mM potassium dihydrogen phosphate, 15% PEG 8000, 20% glycerol, and 2 mM MgSO4 for crystal 1, 10 mM potassium dihydrogen phosphate, 12% PEG 8000, 20% glycerol, and 2 mM MgSO4 for crystal 2, 25 mM potassium dihydrogen phosphate, 14% PEG 8000, and 5 mM LiCl for crystal 3, and 8 mM potassium dihydrogen phosphate, 14% PEG 8000, 20% glycerol, and 5 mM CaCl2 for crystal 4
-
hanging drop vapor diffusion method, in presence of Ca2+, Zn2+ and substrate or product
Q57573
hanging drop vapour diffusion method, best crystals in the presence of Zn2+ and phosphate
Q57573
MJ0109 with bound metal ions, Mg2+, Zn2+, or Mn2+, crystal structure analysis, PDB ID 1DK4
-
hanging drop vapour diffusion method with in 10-14% (v/v) 2-methyl-2,4-pentanediol, 0.1 M tri-sodium citrate, pH 5.6, and 0.2 M ammonium acetate
-
purified recombinant enzyme, sitting drop vapour diffusion method, 24 mg/ml protein in 10 mM Tris-HCl pH 8.0, 50 mM NaCl, 2 mM MgCl2, 5mM DTT is mixed with crystallization solution containing 0.2 M Li2SO4, 20% PEG 3350, 0.1 M HEPES, pH 7.0, method optimization, X-ray diffraction structure determination and analysis at 2.6 A resolution
Q6G709, -
standing drop vapour diffusion method with 15% (w /v) PEG 4000, 15% (v /v) PEG 400, 0.2 M MgSO4, and 50 mM (NH4)2SO4, in 50 mM cacodylate buffer, pH 8
O33832
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
stable at low pH values, inactivated below pH 3
6
9.5
-
about 50% of the maximum activity is retained at pH 6.0 and pH 9.5
8
-
O14732, P29218
the activity of IMPA1 drops to 30% at pH 8.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
stable overnight, enzyme from Sepharose step
37
80
-
-
37
-
-
at 37C IMPase activity of sll1383 shows about 45% of the activity observed at 42C
60
70
-
80-85% of activity retained after 1 h
60
-
-
no loss of activity after 3 h, dialyzed hemolysates
60
-
-
11% and 25% loss of activity after 8 and 15 min
70
-
-
no loss of activity after 30 min
70
-
-
indefinitely stable at
70
-
-
10% of activity lost within 5 min
70
-
-
50% of activity lost within 1 min, Mg2+ stabilizes activity for short periods
70
-
-
2 min, loss of 95% activity
75
-
-
for 10 min, the duodenal enzyme retains only 27% of activity, the brain enzyme 67%
80
-
-
largely destroyed in 1 h
80
-
-
major portion of activity retained after 15 min
85
-
-
for 30 min 95% of activity remains
85
-
-
for 30 min no loss of activity
87
-
-
-
87
-
-
Tm-value
100
-
-
rapidly destroyed at
100
-
-
for 10 min 20-25%, for 30 min 70% loss of activity
additional information
-
-
the archaeal IMPase is extremely stable and active over a wide temperature range
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, in the presence of 0.1 mM GSH, for 4 days
-
at 4C stable for 1 week, after that time 30% loss of activity per week
-
4C, 2-mercaptoethanol or DTT, complete loss of activity after 4 days, no loss of activity then stored in 50 mM Tris-acetate, pH 8 for 1 month
-
4C, no loss of activity for 1 month
-
-20C, stable indefinitely
-
4C, no loss of activity for 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by heat treatment at 85C and QFF resin chromatography
-
Toyopearl Super Q-650S column chromatography, ultracentrifugation, and Sephacryl S-200 gel filtration
-
2000fold
-
2800fold
-
partial
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by ion exchange chromatography, ammonium sulfate fractionation, and dialysis
P20456
high yield purification of recombinant protein from Escherichia coli BL21-(DE3)pLsyS
-
Sephadex Q-Sepharose fast flow column chromatography
-, P0ADG4
Sephacryl S-300 gel filtration, hydroxyapatite column chromatography, and DEAE-Sephacel column chromatography
-
5.4fold
-
HisTrap column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration
-
gel filtration, recombinant protein
B3DFH0, -
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 85C and QFF resin chromatography
-
recombinant protein from Escherichia coli
Q57573
Toyopearl Super Q-650S column chromatography, phenyl-Sepharose column chromatography, ultracentrifugation, and Sephacryl S-200 gel filtration
-
recombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant protein from Escherichia coli using His-tag
-
Sephacryl S200-HR gel filtration
-
100 fold, partial
-
2563.30 fold
-
6000 and 2563fold
-
recombinant protein from Escherichia coli using His-tag
-
recombinant protein from Escherichia coli
-
recombinant His-tagged enzyme to homogeneity from Escherichia coli strain M15 by nickel affinity chromatography and gel filtration
Q6G709, -
412fold
-
from brain
-
Q-Sepharose fast flow column chromatography
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 85C and QFF resin chromatography
-
Sepharose Q FF column chromatography
O33832
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene Impa1, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis, and phylogenetic analysis,
-
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
Q6NPM8, Q94F00, Q9M8S8
genes IMPL2 and VTC4; genes IMPL2 and VTC4; genes IMPL2 and VTC4
Q6NPM8, Q94F00, Q9M8S8
expressed in Eschericha coli inositol monophosphatase deficient strain CG1307, can not complement effects of inositol monophosphatase deficiency
-
expressed in Escherichia coli
-
expressed in Escherichia coli Origami B(DE3) cells
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
overexpression in Escherichia coli
-
expression in Escherichia coli strain BL21(DE3)
P20456
expression in Escherichia coli strain BL21(DE3)pLysS
-
expressed in Eschericha coli inositol monophosphatase deficient strain CG1307, complements effects of inositol monophosphatase deficiency, expressed in Escherichia coli BL21-(DE3)pLsyS
-
expressed in Escherichia coli BL21(DE3) cells
-, P0ADG4
expressed in Escherichia coli strain K-12 AG1
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expression in Escherichia coli strain DH5alpha
-
cDNA library screen, expression in Escherichia coli BL21(DE3), pCR4-TOPO, pET-28b vectors
B3DFH0, -
expressed in Eschericha coli inositol monophosphatase deficient strain CG1307, can not complement effects of inositol monophosphatase deficiency
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli strain BL21(DE3)
-
expression of the MJ109 gene in Escherichia coli
-
expressed in HEK-293T cells; expressed in HEK-293T cells
O14732, P29218
expressed in Escherichia coli
-
gene Rv2131c, expression of soluble N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
genes impA and impC, genetic analysis of the four IMPase homologues that are present in the Mycobacterium tuberculosis genome, real-time quantitative PCR expression analysis
-
expressed in Escherichia coli M15
-
expression in Escherichia coli
-
gene sas2203, DNA and amino acid sequence determination and analysis, recombinant expression of the His-tagged enzyme in Escherichia coli strain M15
Q6G709, -
expressed in Escherichia coli BL-21 (DE3) cells
-
expressed in Eschericha coli inositol monophosphatase deficient strain CG1307, can not complement effects of inositol monophosphatase deficiency
-
expressed in Escherichia coli
O33832
expression in Escherichia coli strain BL21(DE3)
-
overexpression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
increase in mRNA expression in kidney and gill after 2 days after transfer from freshwater to seawater, no expression detected in the intestine
-
up to 17fold increases in mRNA expression and 2fold increases in protein abundance in major osmoregulatory tissues following transfer of fish to seawater
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C150S
-
insensitive toward inactivation with oxygen or thioredoxin, no effect on activity
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
Archaeoglobus fulgidus AF2372
-
insensitive toward inactivation with oxygen or thioredoxin, no effect on activity
-
D87N
-
complete inactivation, resulting enzyme is still able to complement inositol monophosphatase deficiency in Escherichia coli CG1307
G173V
-, P0ADG4
loss of sensitivity to RNA pol binding
H98F
-, P0ADG4
slightly increased kcat value compared to the wild type enzyme
K251A
-, P0ADG4
decreased kcat value compared to the wild type enzyme
L96F/R184I
-, P0ADG4
loss of sensitivity to RNA pol binding
R121A
-, P0ADG4
slightly decreased kcat value compared to the wild type enzyme
R183a
-, P0ADG4
increased kcat value compared to the wild type enzyme
R184A
-, P0ADG4
shift of the monomer-dimer equilibrium toward monomer
R184I
-, P0ADG4
loss of sensitivity to RNA pol binding
R199A
-, P0ADG4
decreased kcat value compared to the wild type enzyme
R248A
-, P0ADG4
strongly increased kcat value compared to the wild type enzyme
V249A
-, P0ADG4
decreased kcat value compared to the wild type enzyme
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
D104N
O14732, P29218
IMPA2 mutant, no activity
D93N
O14732, P29218
IMPA1 mutant, no activity
D104N
-
activity almost completely abolished
D107N
-
activity almost completely abolished
D235N
-
activity almost completely abolished
D40N
-
site-sirected mutagenesis, nearly inactive mutant concerning both inositol monophosphatase and fructose-1,6-bisphosphatase activities
D86N
-
site-directed mutagenesis of gene impC
D94N
-
site-sirected mutagenesis, nearly inactive mutant concerning both inositol monophosphatase and fructose-1,6-bisphosphatase activities
E83D
-
activity almost completely abolished
L71A
-
site-sirected mutagenesis, no decrease in catalytic activity, but the mutant enzyme is 12fold more resistant to inhibition by Li+ compared to the wild-type enzyme
W234L
-
activity almost completely abolished
L81A
-
10fold more resistant towards Li+ inhibition compared to wild type enzyme
additional information
-
construction of deletion mutants of genes impC and impA
D86N
Mycobacterium tuberculosis H37Rv, ATCC 25618
-
site-directed mutagenesis of gene impC
-
additional information
Mycobacterium tuberculosis H37Rv, ATCC 25618
-
construction of deletion mutants of genes impC and impA
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pharmacology
P20456
the enzyme is the putative target of lithium therapy
drug development
-
the enzyme is a target for development of lithium-mimetic agents for the treatment of bipolar disorder, high-throughput cell-based screening using scintillation proximity assay for the discovery of enzyme inhibitors, overview