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(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl cyclohexylammonium 1-hydroxyphosphonate + H2O
?
-
-
-
-
?
(-)-(1R,2R,4R,6R)-2,4,6-trihydroxycyclohexyl-1-hydroxyphosphonate cyclohexylammonium salt + H2O
?
-
-
-
-
?
1-L-chiro-inositol 3-phosphate
1-L-chiro-inositol + phosphate
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
2'-CMP + H2O
cytidine + phosphate
2'-GMP + H2O
guanosine + phosphate
2'-phosphoadenosine 5'-phosphate + H2O
?
2'-UMP + H2O
uridine + phosphate
2,3-diphosphoglycerate + H2O
?
-
-
-
-
?
2-phosphoglycerate + H2O
?
2-phosphoglycerol + H2O
glycerol + phosphate
-
-
-
-
?
2-phosphoglycolate + H2O
?
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
3'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
-
?
3,5-dideoxy-D-myo-inositol 1-phosphate + H2O
3,5-dideoxy-D-myo-inositol + phosphate
3,5-dideoxy-L-myo-inositol 1-phosphate + H2O
3,5-dideoxy-L-myo-inositol + phosphate
3-deoxy-D-myo-inositol 1-phosphate + H2O
3-deoxy-D-myo-inositol + phosphate
3-deoxy-L-myo-inositol 1-phosphate + H2O
3-deoxy-L-myo-inositol + phosphate
3-phosphoglycerate + H2O
?
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
5'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
5'-dAMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
-
-
-
-
?
6-phosphogluconate + H2O
?
-
-
-
-
?
alpha-D-galactose 1-phosphate + H2O
alpha-D-galactose + phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose + phosphate
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
ATP + H2O
ADP + phosphate
-
-
-
-
?
D-alpha-galactose 1-phosphate + H2O
?
-
-
-
-
?
D-alpha-glucose 1-phosphate + H2O
?
-
-
-
-
?
D-beta glucose 1-phosphate + H2O
?
-
-
-
-
?
D-erythrose 4-phosphate + H2O
D-erythrose + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
D-fructose 1-phosphate + H2O
D-fructose + phosphate
D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
D-fructose 6-phosphate + H2O
?
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-galactose 1-phosphate + H2O
D-galactose + phosphate
105% of the activity with D-myo-inositol 1-phosphate
-
-
?
D-glucitol-6-phosphate + H2O
D-glucitol + phosphate
-
hydrolyzed very slowly
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
D-glucose 6-phosphate + H2O
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose-6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-inositol 1-phosphate + H2O
D-inositol + phosphate
-
-
-
-
?
D-mannitol-6-phosphate + H2O
D-mannitol + phosphate
-
hydrolyzed very slowly
-
-
?
D-mannose 6-phosphate + H2O
?
-
-
-
-
?
D-myo-inositol 1,2,3,4,5,6-hexakisphosphate + H2O
D-myo-inositol 1,2,3,4,5-pentakisphosphate + phosphate
-
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
D-myo-inositol 2-phosphate + H2O
D-myo-inositol + phosphate
D-myo-inositol 3-phosphate + H2O
D-myo-inositol + phosphate
D-ribose 5-phosphate + H2O
?
-
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
-
?
D-xylose 5-phosphate + H2O
D-xylose + phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
fructose 1-phosphate + H2O
?
-
-
-
-
?
fructose 6-phosphate + H2O
?
-
-
-
-
?
glucitol 6-phosphate + H2O
glucitol + phosphate
-
-
-
?
glucose 1-phosphate + H2O
?
glycerol 2-phosphate + H2O
glycerol + phosphate
inosine 5'-phosphate + H2O
?
-
-
-
-
?
inositol 1,3-thiophosphate + H2O
?
-
-
-
-
?
inositol 1-phosphate + H2O
inositol + phosphate
inositol 1-phosphate + H2O
myo-inositol + phosphate
inositol 2-phosphate + H2O
?
inositol 4-phosphate + H2O
myo-inositol + phosphate
-
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
?
L-glycerol 1-phosphate + H2O
glycerol + phosphate
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
mannitol 1-phosphate + H2O
mannitol + phosphate
-
-
-
?
myo-inositol 1,3-thiophosphate + H2O
?
-
reaction 3times slower than reaction with inositol 1-phosphate
-
?
myo-inositol 1,4-bisphosphate + H2O
?
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
myo-inositol 2-phosphate + H2O
myo-inositol + phosphate
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
myo-inositol 4-phosphate + H2O
myo-inositol + phosphate
myo-inositol 5-phosphate + H2O
myo-inositol + phosphate
myo-inositol 6-phosphate + H2O
myo-inositol + phosphate
myo-inositol phosphate + H2O
myo-inositol + phosphate
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
phosphatidylinositol 4,5-bisphosphate + H2O
?
-
-
-
-
?
phosphatidylinositol 4-phosphate + H2O
phosphatidylinositol + phosphate
-
-
-
?
propan-1-ol 2-phosphate + H2O
1-propanol + phosphate
-
-
-
-
?
purine nucleotides + H2O
?
-
-
-
-
?
pyrimidine ribonucleotides + H2O
?
-
-
-
-
?
scyllo-inositol 1-phosphate + H2O
scyllo-inositol + phosphate
IMPA1 shows strong activity towards scyllo-inositol 1-phosphate, whereas IMPA2 shows almost no affinity
-
-
?
additional information
?
-
2'-AMP + H2O
adenosine + phosphate
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
2'-AMP + H2O
adenosine + 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
-
?
2'-AMP + H2O
adenosine + phosphate
600% of the rate with inositol 1-phosphate
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
-
18% of the rate with inositol 1-phosphate
-
?
2'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
2'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
2'-CMP + H2O
cytidine + phosphate
-
-
-
-
?
2'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
2'-GMP + H2O
guanosine + phosphate
-
-
-
-
?
2'-phosphoadenosine 5'-phosphate + H2O
?
-
-
-
?
2'-phosphoadenosine 5'-phosphate + H2O
?
-
-
-
-
?
2'-UMP + H2O
uridine + phosphate
-
-
-
-
?
2'-UMP + H2O
uridine + phosphate
-
-
-
-
?
2-phosphoglycerate + H2O
?
-
-
-
-
?
2-phosphoglycerate + H2O
?
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3,5-dideoxy-D-myo-inositol 1-phosphate + H2O
3,5-dideoxy-D-myo-inositol + phosphate
-
-
-
-
?
3,5-dideoxy-D-myo-inositol 1-phosphate + H2O
3,5-dideoxy-D-myo-inositol + phosphate
-
-
-
?
3,5-dideoxy-D-myo-inositol 1-phosphate + H2O
3,5-dideoxy-D-myo-inositol + phosphate
-
-
-
-
?
3,5-dideoxy-L-myo-inositol 1-phosphate + H2O
3,5-dideoxy-L-myo-inositol + phosphate
-
-
-
-
?
3,5-dideoxy-L-myo-inositol 1-phosphate + H2O
3,5-dideoxy-L-myo-inositol + phosphate
-
-
-
?
3,5-dideoxy-L-myo-inositol 1-phosphate + H2O
3,5-dideoxy-L-myo-inositol + phosphate
-
-
-
-
?
3-deoxy-D-myo-inositol 1-phosphate + H2O
3-deoxy-D-myo-inositol + phosphate
-
-
-
-
?
3-deoxy-D-myo-inositol 1-phosphate + H2O
3-deoxy-D-myo-inositol + phosphate
-
-
-
-
?
3-deoxy-L-myo-inositol 1-phosphate + H2O
3-deoxy-L-myo-inositol + phosphate
-
-
-
-
?
3-deoxy-L-myo-inositol 1-phosphate + H2O
3-deoxy-L-myo-inositol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
very effective substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
very effective substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
high rate of hydrolysis
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
very effective substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
very effective substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
very effective substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + 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
-
-
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
-
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
-
-
?
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
-
-
?
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
-
-
-
?
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 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
very effective substrate
-
?
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
-
-
-
?
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 1-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
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
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
?
-
-
-
-
?
D-glucose 6-phosphate + H2O
?
-
-
-
-
?
D-glucose 6-phosphate + H2O
?
-
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
?
-
-
-
?
D-myo-inositol 1,4-bisphosphate + H2O
?
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
substrate binding structure, interactions sites with the enzyme involving Tyr155 and Ala172
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
catalytic mechanism and substrate-enzyme interactions
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
preferred substrate
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
IMPA1 shows strong activity towards D-myo-inositol 1-phosphate, whereas IMPA2 shows significantly lower affinity
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 1-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 2-phosphate + H2O
D-myo-inositol + phosphate
18.8% of the activity with D-myo-inositol 1-phosphate
-
-
?
D-myo-inositol 2-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
?
D-myo-inositol 2-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 3-phosphate + H2O
D-myo-inositol + phosphate
17.8% of the activity with D-myo-inositol 1-phosphate
-
-
?
D-myo-inositol 3-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
D-myo-inositol 3-phosphate + H2O
D-myo-inositol + phosphate
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
-
-
-
-
?
DL-myo-inositol 1-phosphate + H2O
DL-myo-inositol + phosphate
-
-
-
-
?
glucose 1-phosphate + H2O
?
-
-
-
-
?
glucose 1-phosphate + H2O
?
-
high rate of hydrolysis
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
39.7% of the activity with D-myo-inositol 1-phosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
64% of the rate with inositol 1-phosphate
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
-
-
-
?
inositol 1-phosphate + H2O
inositol + phosphate
-
-
-
?
inositol 1-phosphate + H2O
inositol + phosphate
-
-
-
?
inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
inositol 2-phosphate + H2O
?
-
-
-
-
?
inositol 2-phosphate + H2O
?
-
-
-
-
?
L-chiro-inositol-3-phosphate + H2O
?
-
-
-
-
?
L-chiro-inositol-3-phosphate + H2O
?
-
-
-
-
?
L-glycerol 1-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
L-glycerol 1-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
L-glycerol 1-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
L-glycerol 1-phosphate + H2O
glycerol + phosphate
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
-
?
L-myo-inositol 1-phosphate + H2O
L-myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
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
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
inversion of phosphate configuration
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
involved in phosphatidylinositol signaling pathway
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
D- and L-isomer, 2.5-fold higher activity with D-isomer
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
very low concentration of inositol compounds
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
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
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
synthesis of myo-inositol, that is a key substrate for synthesis of phosphatidylinositol
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
key metabolic step, de novo synthesis of myo-inositol, phosphatidylinositol is essential of growth
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
key metabolic step, de novo synthesis of myo-inositol, phosphatidylinositol is essential of growth
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
de novo biosynthesis of inositol precursor of inositol phospholipids
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
reguglation of exopolysaccharide synthesis suggested
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
D- and L-isomer serve as substrate
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
de novo biosynthesis of inositol, involved in phosphoinositide signaling pathway
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
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
-
acts on D- and L-isomer
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
regulation of phosphatidylinositol signaling pathway
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
organism do not contain lipids with inositol head group, involved in the response to thermal stress
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
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 2-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 2-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
-
-
inversion of phosphate configuration
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol 3-phosphate + H2O
myo-inositol + phosphate
-
the substrate shows a similar binding structure as inositol 5-phosphate
-
-
?
myo-inositol 4-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol 4-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 5-phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol 5-phosphate + H2O
myo-inositol + phosphate
-
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
-
-
-
-
?
myo-inositol 6-phosphate + H2O
myo-inositol + phosphate
-
the substrate shows a similar binding structure as inositol 5-phosphate
-
-
?
myo-inositol phosphate + H2O
myo-inositol + phosphate
-
highest activity
-
-
?
myo-inositol phosphate + H2O
myo-inositol + phosphate
-
highest activity
-
-
?
myo-inositol phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol phosphate + H2O
myo-inositol + phosphate
-
-
-
-
?
myo-inositol phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol phosphate + H2O
myo-inositol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
the reaction is only catalyzed in the presence of ZnCl2 at acidic pH
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
additional information
?
-
-
the enzyme shows 5-20% activity for D-myo-inositol 1,4-bisphophate, D-fructose 1,6-diphosphate, 3'-phosphoadenosine 5'-phosphate, 3'-phospho phosphoadenosine-5?-phosphosulfate, ATP, AMP, ADP and NADP+ compared to myo-inositol phosphate
-
-
?
additional information
?
-
-
the enzyme shows 5-20% activity for D-myo-inositol 1,4-bisphophate, D-fructose 1,6-diphosphate, 3'-phosphoadenosine 5'-phosphate, 3'-phospho phosphoadenosine-5?-phosphosulfate, ATP, AMP, ADP and NADP+ compared to myo-inositol phosphate
-
-
?
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
?
-
at temperatures above 80°C the organism accumulates di-myo-inositol 1,1'-phosphate as a compatible solute which is regulated by the temperature dependence of the substrate affinity
-
-
?
additional information
?
-
-
at temperatures above 80°C the organism accumulates di-myo-inositol 1,1'-phosphate as a compatible solute which is regulated by the temperature dependence of the substrate affinity
-
-
?
additional information
?
-
the enzyme also shows low fructose bisphosphatase activity
-
-
?
additional information
?
-
-
the enzyme also shows low fructose bisphosphatase activity
-
-
?
additional information
?
-
D-myo-inositol-1,4,5-triphosphate, D-glucose 6-phosphate, D-fructose 6-phosphate, NAD+, FMN+, bis-p-nitrophenyl diphosphate, ADP and ATP are no substrates
-
-
?
additional information
?
-
-
D-myo-inositol-1,4,5-triphosphate, D-glucose 6-phosphate, D-fructose 6-phosphate, NAD+, FMN+, bis-p-nitrophenyl diphosphate, ADP and ATP are no substrates
-
-
?
additional information
?
-
the enzyme also exhibits high phosphatase activities toward NADP(H) and toward 2'-AMP and 2'-phosphoadenosine 5'-phosphate, but not toward 3'-AMP, 3'-phosphoadenosine 5'-phosphate, and 5'-AMP
-
-
?
additional information
?
-
-
the enzyme also exhibits high phosphatase activities toward NADP(H) and toward 2'-AMP and 2'-phosphoadenosine 5'-phosphate, but not toward 3'-AMP, 3'-phosphoadenosine 5'-phosphate, and 5'-AMP
-
-
?
additional information
?
-
-
archeal enzyme displays inositol monophosphatase as well as fructose 1,6-bisphosphatase activity
-
?
additional information
?
-
-
archeal enzyme displays inositol monophosphatase as well as fructose 1,6-bisphosphatase activity
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
triphosphoinositide
-
-
?
additional information
?
-
the enzyme is the key enzyme of the phosphatidylinositol signalling pathway and the putative target of the mood-stabilizing drug lithium
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of the phosphatidylinositol signalling pathway and the putative target of the mood-stabilizing drug lithium
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl phosphate, 5'-AMP, NAD+, glucose 1-phosphate and glucose 6-phosphate
-
?
additional information
?
-
-
traces of activity with glucose 1-phosphate, no activity with 4-nitrophenyl phosphate and fructose 1,6-bisphosphate
-
?
additional information
?
-
-
small activity: 5-ribonucleotides
-
-
?
additional information
?
-
-
does not hydrolyze p-nitrophenyl phosphate, ADP, AMP or D-glucose 6-phosphate
-
-
?
additional information
?
-
-
the enzyme is involved in development of bipolar disorder
-
-
?
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
?
-
-
not: inorganic phosphate, myo-inositol pentaphosphate
-
-
?
additional information
?
-
no substrate: D-myo-inositol-1-phosphate
-
-
?
additional information
?
-
-
no substrate: D-myo-inositol-1-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
-
-
?
additional information
?
-
D-glucose 6-phosphate, D-fructose 6-phosphate, 5'-AMP and NAD+ are not hydrolyzed
-
?
additional information
?
-
selctive for phosphatidylinositol 4-phosphate, no reaction with other phosphatidylinositols tested
-
-
?
additional information
?
-
-
substrate specificity, enzyme is both inositol monophosphatase and fructose-1,6-bisphosphatase
-
-
?
additional information
?
-
-
substrate specificity, enzyme is both inositol monophosphatase and fructose-1,6-bisphosphatase
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
avian and plant enzyme attack myo-inositol 2-phosphate, mammalian enzyme not
-
-
?
additional information
?
-
-
not: inositol 2-phosphate, inositol 1,4-bisphosphate, inositol 1,4,5-triphosphate
-
-
?
additional information
?
-
-
traces of activity with glucose 1-phosphate and 4-nitrophenylphosphate, no activity with glucose 6-phosphate and 5'-AMP
-
?
additional information
?
-
-
no activity with glucose 6-phosphate and 5'-AMP
-
?
additional information
?
-
-
key enzyme in the phosphoinositide cell-signaling system
-
-
?
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
-
?
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(-)-(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
2,3,7-trihydroxycyclohepta-2,4,6-trien-1-one
-
-
2-deoxyglucose-6-phosphate
-
-
3-phosphoglycerate
-
weak competetive inhibitor
6-phosphogluconate
-
slight
Carbachol
-
in combination with Li
CO2
enzyme dimers in the presence of CO2 or formaldehyde form mutual, methylene-bridged cross-links between Lys158 and Cys245 residues
Cr2+
-
50% inhibition at 3 mM
Dimethylsulfoxide
-
5% inhibition
DL-myo-inositol 1-phosphate
-
formaldehyde
enzyme dimers in the presence of CO2 or formaldehyde form mutual, methylene-bridged cross-links between Lys158 and Cys245 residues
iodoacetate
-
30% inhibition at 10 mM
L-690488
-
a tetrapivaloyloxymethyl ester prodrug of L-690330
monoclonal antibody [DV1]
-
one of five antibodies was found to inhibit the enzyme activity
-
myo-inositol 1,3,4,5,6 pentakis(dihydrogen phosphate)
-
-
myo-Inositol tetrakis(dihydrogen phosphate)
-
-
N-ethylmaleimide
-
substrate and Mg2+ protect
Na2MoO4
-
30% inhibition at 10 mM
O2
-
activity of the native enzyme but not the C150S mutant can be completely abolished with oxygen, reversible with thiol-containing compounds
Phenylmercuric nitrate
-
-
PO43-
competitive inhibition
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
thioredoxin
-
inhibits native enzyme but nut C150S mutant
1-(4-hydroxyphenyloxy)ethane-1,1-bisphosphonic acid
-
L-690,330
1-(4-hydroxyphenyloxy)ethane-1,1-bisphosphonic acid
-
-
Be2+
-
-
Be2+
-
50% inhibition at 0.09 mM
Ca2+
-
-
Ca2+
-
50% inhibition at 0.4 mM
Ca2+
-
Ca2+/EGTA buffer, not: 0.0001-0.01 mM
Ca2+
-
strong competitive against Mg2+
Ca2+
-
inhibits only at millimolar concentrations
Co2+
-
inhibits hydrolysis of inositol-1-phosphate at high concentrations
Co2+
-
50% inhibition at 0.7 mM
Cu2+
-
CuSO4
Cu2+
-
50% inhibition at 1 mM
F-
-
50% inhibitory at 1 mM
HgCl2
-
-
HgCl2
-
95% inhibition at 1 mM
KF
-
-
L-690330
-
bisphosphonate enzyme inhibitor
L-690330
bisphosphonate substrate-based inhibitor
Li+
-
IMPA1 is moderately sensitive to lithium
Li+
binding structure, modelling of the lithium-inhibited enzyme-product complex
Li+
-
lithium impairs neuronal phosphatidylinositol 4,5-bisphosphate synthesis through inhibition of the enzyme
Li+
-
strongly inhibited by Li+ (complete inhibition at 2 mM)
Li+
-
1.25 mM is 50% inhibitory
Li+
0-4 mM LiCl, 3 mM Li+ inhibits activity by approximately 50%, inhibition increases with Li+ concentration
Li+
-
substantial inhibition at 250 mM
Li+
-
250 mM inhibits about 65%, 1000 mM about 90%
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
Li+
-
50% inhibition at 0.9 mM
Li+
-
inhibitory, but can amplify the effect of Mg2+
Li+
-
50% inhibition at 0.8 mM, also able to inhibit cell growth
Li+
-
inhibits 50% of activity at 1 mM, uncompetitive inhibitor
Li+
-
inhibits at millimolar concentrations
Li+
-
different Li-isotopes do not possess differential lethality effects in vivo
Li+
-
at 100 mM 72% inhibition of the brain enzyme but only 27% of the duodenal enzyme
Li+
-
presence of lithium reduces IMPase activity by 20% and 60% in the wild type and in the constitutively active Ras1 mutant, respectively
Li+
competitive inhibitor of the cofactor Mg2+
Li+
-
50% inhibitory at 100 mM
LiCl
-
Mg2+
-
inhibits hydrolysis of inositol-1-phosphate at high concentrations
Mg2+
inhibitory at high concentrations
Mg2+
-
activity is significantly reduced at high concentrations of Mg2+
Mg2+
-
tight binding of Mg2+ to the protein affects the secondary structure
Mg2+
uncompetitive inhibitor at high concentrations
Mg2+
-
slight inhibition at 100 mM
Mn2+
-
-
Mn2+
-
50% inhibition at 0.8 mM
Mn2+
-
strong competitive against Mg2+
Mn2+
-
inhibits only at millimolar concentrations
myo-inositol
-
non-competitive inhibition
myo-inositol
-
product inhibition, competitive
myo-inositol
non-competitive inhibition
Na+
-
50% inhibition at 70 mM
NaF
-
90% inhibition by 10 mM
NaF
-
45% inhibition at 1 mM
NaF
-
inhibits by 60% and 100% at 1 mM and 5 mM respectively
Ni2+
-
-
Ni2+
-
50% inhibition at 30 mM
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
phosphate
-
-
phosphate
-
product inhibition, competitive
phosphate
-
product inhibition, competitive
SO42-
-
40% inhibitory at 17 mM
SO42-
-
hydrolyzed very slowly
sulfhydryl reagents
-
-
Zn2+
-
ZnCl2
Zn2+
-
50% inhibition at 0.005 mM
additional information
-
not inhibited by Na+ or K+
-
additional information
300 mM Na+ or K+have no effect
-
additional information
-
300 mM Na+ or K+have no effect
-
additional information
-
potency and structural features of product-like inhibitors, inhibitory mechanism, overview
-
additional information
-
not inhibited by butanedione monoxime, or orthovanadate
-
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
-
Li+, glycerol and glucose in the culture medium depresses enzyme expression, no inhibition with valproate
-
additional information
-
Na+, K+, NH4+ have no significant effect on the enzyme activity
-
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Alzheimer Disease
Alteration of myo-inositol monophosphatase in Alzheimer's disease brains.
Arthritis
Immune myopathies with perimysial pathology: Clinical and laboratory features.
Breast Neoplasms
A novel oncogenic role of inositol phosphatase SHIP2 in ER-negative breast cancer stem cells: involvement of JNK/vimentin activation.
Breast Neoplasms
Regulation of PtdIns(3,4,5)P3/Akt signalling by inositol polyphosphate 5-phosphatases.
Carcinoma
A novel function of IMPA2, plays a tumor-promoting role in cervical cancer.
Carcinoma
Conserved synteny between the Fugu and human PTEN locus and the evolutionary conservation of vertebrate PTEN function.
Carcinoma
Decreased cyclic inositol phosphohydrolase activity in hamster renal tumors and human renal cell carcinomas.
Carcinoma
IMPA2 Downregulation Enhances mTORC1 Activity and Restrains Autophagy Initiation in Metastatic Clear Cell Renal Cell Carcinoma.
Carcinoma in Situ
A novel function of IMPA2, plays a tumor-promoting role in cervical cancer.
Carcinoma, Renal Cell
Decreased cyclic inositol phosphohydrolase activity in hamster renal tumors and human renal cell carcinomas.
Carcinoma, Renal Cell
IMPA2 Downregulation Enhances mTORC1 Activity and Restrains Autophagy Initiation in Metastatic Clear Cell Renal Cell Carcinoma.
Cardiomegaly
Inpp5f Is a Polyphosphoinositide Phosphatase That Regulates Cardiac Hypertrophic Responsiveness.
Cardiomyopathies
[Evolution and thromboembolic complications of the idiopathic peripartal cardiomyopathy at Dakar University Hospital: forward-looking study about 33 cases].
Cardiovascular Diseases
[Treatment of erectile dysfunction in patients with ischemic heart disease and angina of effort]
Chronic Periodontitis
Upregulation of immunoregulatory Src homology 2 molecule containing inositol phosphatase and mononuclear cell hyporesponsiveness in oral mucosa during chronic periodontitis.
Dementia
Inositol monophosphatase activity in normal, Down syndrome and dementia of the Alzheimer type CSF.
Dementia, Multi-Infarct
Inositol monophosphatase activity in normal, Down syndrome and dementia of the Alzheimer type CSF.
Dermatomyositis
Immune myopathies with perimysial pathology: Clinical and laboratory features.
Diabetes Mellitus, Type 2
Hyperglycemia and hyperlipidemia blunts the Insulin-Inpp5f negative feedback loop in the diabetic heart.
Diabetes, Gestational
Placental Inositol Reduced in Gestational Diabetes as Glucose Alters Inositol Transporters and IMPA1 Enzyme Expression.
Diabetic Cardiomyopathies
Hyperglycemia and hyperlipidemia blunts the Insulin-Inpp5f negative feedback loop in the diabetic heart.
Down Syndrome
Inositol monophosphatase activity in normal, Down syndrome and dementia of the Alzheimer type CSF.
Drug Resistant Epilepsy
Inositol phosphatase INPP4A inhibits the apoptosis of in vitro neurons with characteristic of intractable epilepsy by reducing intracellular Ca2+ concentration.
Epilepsy
Impaired neuronal activity and differential gene expression in STXBP1 encephalopathy patient iPSC-derived GABAergic neurons.
Erectile Dysfunction
[An open non-comparative study of impase for treating erectile dysfunction]
Erectile Dysfunction
[Correction of erectile dysfunction in patients with chronic abacterial prostatitis].
Erectile Dysfunction
[Impase in the treatment of erectile dysfunction]
Erectile Dysfunction
[Treatment of erectile dysfunction in patients with ischemic heart disease and angina of effort]
Erectile Dysfunction
[Use of impase in the therapy of erectile dysfunction]
Erectile Dysfunction
[Viagra, cialis, impase--which of them, to whom, when and how?]
Galactosemias
Expression of human inositol monophosphatase suppresses galactose toxicity in Saccharomyces cerevisiae: possible implications in galactosemia.
Glioblastoma
Inositol Polyphosphate-5-Phosphatase F (INPP5F) inhibits STAT3 activity and suppresses gliomas tumorigenicity.
Glioma
Inositol Polyphosphate-5-Phosphatase F (INPP5F) inhibits STAT3 activity and suppresses gliomas tumorigenicity.
Glioma
Lithium inhibits invasion of glioma cells; possible involvement of glycogen synthase kinase-3.
Heart Defects, Congenital
Imprinting aberrations of SNRPN, ZAC1 and INPP5F genes involved in the pathogenesis of congenital heart disease with extracardiac malformations.
Hepatitis, Alcoholic
Antioxidant and hepatoprotective effects of intracellular mycelium polysaccharides from Pleurotus geesteranus against alcoholic liver diseases.
Huntington Disease
Potential protective effects of autophagy activated in MPP+ treated astrocytes.
Hyperglycemia
Hyperglycemia and hyperlipidemia blunts the Insulin-Inpp5f negative feedback loop in the diabetic heart.
Hyperlipidemias
Hyperglycemia and hyperlipidemia blunts the Insulin-Inpp5f negative feedback loop in the diabetic heart.
Hypertension, Pulmonary
Inositol monophosphatase 1 as a novel interacting partner of RAGE in pulmonary hypertension.
Infections
Effects of the deletion and over-expression of Fusarium graminearum gene FgHal2 on host response to mycovirus Fusarium graminearum virus 1.
Infections
Macrophage pro-inflammatory response to Francisella novicida infection is regulated by SHIP.
Infections
The inositol phosphatase SHIP controls Salmonella enterica serovar Typhimurium infection in vivo.
inositol-phosphate phosphatase deficiency
Inositol monophosphatase 1 (IMPA1) mutation in intellectual disability patients impairs neurogenesis but not gliogenesis.
Intellectual Disability
A homozygous loss-of-function mutation in inositol monophosphatase 1 (IMPA1) causes severe intellectual disability.
Intellectual Disability
Inositol monophosphatase 1 (IMPA1) mutation in intellectual disability patients impairs neurogenesis but not gliogenesis.
Intellectual Disability
Loss-of-function mutation in inositol monophosphatase 1 (IMPA1) results in abnormal synchrony in resting-state EEG.
Ischemic Stroke
IMPA2 polymorphisms and risk of ischemic stroke in a northwest Han Chinese population.
Leukemia, Lymphocytic, Chronic, B-Cell
Gene expression of INPP5F as an independent prognostic marker in fludarabine-based therapy of chronic lymphocytic leukemia.
Lung Diseases, Interstitial
Immune myopathies with perimysial pathology: Clinical and laboratory features.
Lung Neoplasms
Increased expression of insulin-like growth factor-II messenger RNA-binding protein 1 is associated with tumor progression in patients with lung cancer.
Malnutrition
Effects of neonatal undernutrition and subsequent nutritional rehabilitation or administration of thyroxine and hydrocortisone on the inositol phosphatase activities in rat intestine.
Malnutrition
Effects of postweaning protein malnutrition on intestinal inositol phosphatase activities in normally weaned and neonatally undernourished rats.
Mania
Inositol deficiency diet and lithium effects.
Melanoma
Regulation of PtdIns(3,4,5)P3/Akt signalling by inositol polyphosphate 5-phosphatases.
Muscular Diseases
Immune myopathies with perimysial pathology: Clinical and laboratory features.
Muscular Dystrophies
Fine mapping of the muscular dystrophy (AM) gene on chicken chromosome 2q.
Neoplasm Metastasis
A novel function of IMPA2, plays a tumor-promoting role in cervical cancer.
Neoplasm Metastasis
Dysregulation of the miR-25-IMPA2 axis promotes metastatic progression in clear cell renal cell carcinoma.
Neoplasms
A novel function of IMPA2, plays a tumor-promoting role in cervical cancer.
Neoplasms
Decreased cyclic inositol phosphohydrolase activity in hamster renal tumors and human renal cell carcinomas.
Neoplasms
Dysregulation of the miR-25-IMPA2 axis promotes metastatic progression in clear cell renal cell carcinoma.
Neoplasms
Increased expression of insulin-like growth factor-II messenger RNA-binding protein 1 is associated with tumor progression in patients with lung cancer.
Neoplasms
Inhibition of vascular smooth muscle cell proliferation, migration, and survival by the tumor suppressor protein PTEN.
Neoplasms
Inositol Polyphosphate-5-Phosphatase F (INPP5F) inhibits STAT3 activity and suppresses gliomas tumorigenicity.
Neoplasms
Overexpression of miR-155 causes expansion, arrest in terminal differentiation and functional activation of mouse natural killer cells.
Neoplasms
Predicting which children are at risk for ependymoma relapse.
Neoplasms
Regulation of PtdIns(3,4,5)P3/Akt signalling by inositol polyphosphate 5-phosphatases.
Neuralgia
Effect of HDAC2/Inpp5f on neuropathic pain and cognitive function through regulating PI3K/Akt/GSK-3? signal pathway in rats with neuropathic pain.
Neuralgia
Pregabalin on Hdac2 and Inpp5f levels in rats with CCI-induced neuropathic pain.
Neuroblastoma
Beryllium competitively inhibits brain myo-inositol monophosphatase, but unlike lithium does not enhance agonist-induced inositol phosphate accumulation.
Neurodegenerative Diseases
Potential protective effects of autophagy activated in MPP+ treated astrocytes.
Obesity
An investigation of obesity susceptibility genes in Northern Han Chinese by targeted resequencing.
Oculocerebrorenal Syndrome
IPIP27 Coordinates PtdIns(4,5)P2 Homeostasis for Successful Cytokinesis.
Parkinson Disease
Association of four new candidate genetic variants with Parkinson's disease in a Han Chinese population.
Raynaud Disease
Immune myopathies with perimysial pathology: Clinical and laboratory features.
Seizures
Effects of the putative lithium mimetic ebselen on pilocarpine-induced neural activity.
Seizures
Hippocampal transcriptional and neurogenic changes evoked by combination yohimbine and imipramine treatment.
Seizures
IMPA1 is essential for embryonic development and lithium-like pilocarpine sensitivity.
Seizures
Inositol-deficient food augments a behavioral effect of long-term lithium treatment mediated by inositol monophosphatase inhibition: an animal model with relevance for bipolar disorder.
Seizures
Intracerebroventricular antisense to inositol monophosphatase-1 reduces enzyme activity but does not affect Li-sensitive behavior.
Seizures
Modulation of phosphatidylinositol turnover on central nicotinic receptors.
Seizures
The inositol monophosphatase inhibitor L-690,330 affects pilocarpine-behavior and the forced swim test.
Seizures
Ziskind-Somerfeld Research Award 1993. Biochemical, behavioral, and clinical studies of the role of inositol in lithium treatment and depression.
Seizures, Febrile
Crystal structure of human myo-inositol monophosphatase 2, the product of the putative susceptibility gene for bipolar disorder, schizophrenia, and febrile seizures.
Seizures, Febrile
Genetic variants in the IMPA2 gene do not confer increased risk of febrile seizures in Caucasian patients.
Seizures, Febrile
Linkage and association of febrile seizures to the IMPA2 gene on human chromosome 18.
Seizures, Febrile
Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1.
Spinal Cord Injuries
Gene-Silencing Screen for Mammalian Axon Regeneration Identifies Inpp5f (Sac2) as an Endogenous Suppressor of Repair after Spinal Cord Injury.
Spinocerebellar Ataxias
Bergmann glial S100B activates myo-inositol monophosphatase 1 and Co-localizes to purkinje cell vacuoles in SCA1 transgenic mice.
Thrombosis
[Evolution and thromboembolic complications of the idiopathic peripartal cardiomyopathy at Dakar University Hospital: forward-looking study about 33 cases].
Tuberculosis
Dimerization of inositol monophosphatase Mycobacterium tuberculosis SuhB is not constitutive, but induced by binding of the activator Mg2+
Tuberculosis
Inositol monophosphate phosphatase genes of Mycobacterium tuberculosis.
Tuberculosis
Purification and biochemical characterization of Mycobacterium tuberculosis SuhB, an inositol monophosphatase involved in inositol biosynthesis.
Uterine Cervical Neoplasms
A novel function of IMPA2, plays a tumor-promoting role in cervical cancer.
Virus Diseases
Impaired B cell function during viral infections due to PTEN-mediated inhibition of the PI3K pathway.
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Naccarato, W.F.; Ray, R.E.; Wells, W.W.
Biosynthesis of myo-inositol in rat mammary gland. Isolation and properties of the enzymes
Arch. Biochem. Biophys.
164
194-201
1974
Rattus norvegicus
brenda
Eisenberg jr., F.; Parthasarathy, R.
Measurement of biosynthesis of myo-inositol from glucose 6-phosphate
Methods Enzymol.
141
127-143
1987
Rattus norvegicus
brenda
Attwood, P.V.; Ducep, J.B.; Chanal, M.C.
Purification and properties of myo-inositol-1-phosphatase from bovine brain
Biochem. J.
253
387-394
1988
Bos taurus
brenda
Shute, J.K.; Baker, R.; Billington, D.C.; Gani, D.
Mechanism of the myo-inositol phosphatase reaction
J. Chem. Soc. Chem. Commun.
1988
626-628
1988
Bos taurus
-
brenda
Shute, J.K.; Baker, R.; Billington, D.C.; Gani, D.
Mechanism of the myo-inositol phosphatase reaction
J. Chem. Soc. Chem. Commun.
1988
422-423
1988
Bos taurus
-
brenda
Ragan, C.I.; Watling, K.J.; Gee, N.S.; Aspley, S.; Jackson, R.G.; Reid, G.G.; Baker, R.; Billington, D.C.; Barnaby, R.J.; Leeson, P.D.
The dephosphorylation of inositol 1,4-bisphosphate to inositol in liver and brain involves two distinct Li+-sensitive enzymes and proceeds via inositol 4-phosphate
Biochem. J.
249
143-148
1988
Bos taurus, Rattus norvegicus
brenda
Carey, F.; Creba, J.A.; French, P.J.; Short, A.D.; Walters, M.; Wayne, J.
Partial purification and characterization of rat brain myo-inositol-1-phosphatase
Biochem. Soc. Trans.
15
429-430
1988
Rattus norvegicus
-
brenda
Takimoto, K.; Okada, M.; Matsuda, Y.; Nakagawa, H.
Purification and properties of myo-inositol-1-phosphatase from rat brain
J. Biochem.
98
363-370
1985
Rattus norvegicus
brenda
Gumber, S.C.; Loewus, M.W.; Loewus, F.A.
Further studies on myo-inositol-1-phosphatase from the pollen of Lilium longiflorum Thunb.
Plant Physiol.
76
40-44
1984
Lilium longiflorum
brenda
Loewus, M.W.; Loewus, F.A.
Myo-inositol-1-phosphatase from the pollen of Lilium longiflorum Thunb.
Plant Physiol.
70
765-770
1982
Lilium longiflorum
brenda
Roth, S.C.; Harkness, D.R.; Isaacks, R.E.
Studies on avian erythrocyte metabolism: purification and properties of myo-inositol 1-phosphatase from chick erythrocytes
Arch. Biochem. Biophys.
210
465-473
1981
Gallus gallus
brenda
Hallcher, L.M.; Sherman, W.R.
The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain
J. Biol. Chem.
255
10896-10901
1980
Bos taurus
brenda
Eisenberg, F.Jr.
D-myoinositol 1-phosphate as product of cyclization of glucose 6-phosphate and substrate for a specific phosphatase in rat testis
J. Biol. Chem.
242
1375-1382
1967
Rattus norvegicus
brenda
Charalampous, F.; Chen, I.W.
Inositol 1-phosphate synthetase and inositol 1-phosphatase from yeast
Methods Enzymol.
9
698-704
1966
Cyberlindnera jadinii
-
brenda
Creba, J.A.; Carey, F.; McCulloch, A.
Metabolism of inositol 1-phosphate in HL60 cells
Biochem. Soc. Trans.
16
557-558
1988
Homo sapiens
-
brenda
Huckle, W.R.; Conn, P.M.
Use of lithium ion in measurement of stimulated pituitary inositol phospholipid turnover
Methods Enzymol.
141
149-155
1987
Rattus norvegicus
brenda
Downes , C.P.; Stone, M.A.
Lithium-induced reduction in intracellular inositol supply in cholinergically stimulated parotid gland
Biochem. J.
234
199-204
1986
Rattus norvegicus
brenda
Huang, E.M.; Detwiler, T.C.
The effects of lithium on platelet phosphoinositide metabolism
Biochem. J.
236
895-901
1986
Homo sapiens
brenda
Conolly, T.M.; Wilson, D.B.; Bross, T.E.; Majerus, P.W.
Isolation and characterization of the inositol cyclic phosphate products of phosphoinositide cleavage by phospholipase C
J. Biol. Chem.
261
122-126
1986
Homo sapiens, Rattus norvegicus
brenda
vom Dahl, S.; Graf, P.; Sies, H.
Hepatic inositol release upon hormonal stimulation of perfused rat liver
Biochem. J.
251
843-848
1988
Rattus norvegicus
brenda
Eisenberg, F.Jr.; Parthasarathy, R.
Myo-inositol 1-phosphate
Methods Enzymol.
6
371-375
1984
Rattus norvegicus
-
brenda
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
brenda
Parthasarathy, L.; Vadnal, R.E.; Ramesh, T.G.; Shyamaladevi, C.S.; Parhasarathy, R.
myo-Inositol monophosphatase from rat testes: purification and properties
Arch. Biochem. Biophys.
304
94-101
1993
Rattus norvegicus
brenda
Parhasarathy, R.; Parhasarathy, L.; Ramesh, T.G.; Shyamaladevi, C.S.; Vadnal, R.E.
The effects of lithium isotopes on the myo-inositol 1-phosphatase reaction in rat brain, liver, and testes
Life Sci.
50
1445-1450
1992
Rattus norvegicus
brenda
Strasser, F.; Pelton, P.D.; Ganzhorn, A.J.
Kinetic characterization of enzyme forms involved in metal ion activation and inhibition of myo-inositol monophosphatase
Biochem. J.
307
585-593
1995
Bos taurus
brenda
McAllister, G.; Whiting, P.; Hammond, E.A.; Knowles, M.R.; Atack, J.R.; Bailey, F.J.; Maigetter, R.; Ragan, C.I.
cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme
Biochem. J.
284
749-754
1992
Bos taurus, Homo sapiens, Rattus norvegicus
brenda
Chen, L.; Roberts, M.F.
Characterization of a tetrameric inositol monophosphatase from the hyperthermophilic bacterium Thermotoga maritima
Appl. Environ. Microbiol.
65
4559-4567
1999
Thermotoga maritima
brenda
Vincendon, P.; Corti, E.; Guindani, A.; Brunati, C.; Sponga, F.; Stefanelli, S.; Denaro, M.; Pelton, P.; Ganzhorn, A.; Islam, K.
An automated high volume assay to screen for inhibitors of myo-inositol monophosphatase from microbial fermentation broths
J. Antibiot.
49
710-712
1996
Homo sapiens
brenda
Stefanelli, S.; Sponga, F.; Ferrari, P.; Sottani, C.; Corti, E.; Brunati, C.; Islam, K.
Inhibitors of myo-inositol monophosphatase, ATCC 20928 factors A and C. Isolation, physico-chemical characterization and biological properties
J. Antibiot.
49
611-616
1996
More
brenda
Ganzhorn, A.J.; Vincendon, P.; Pelton, J.T.
Structural characterization of myo-inositol monophosphatase from bovine brain by secondary structure prediction, fluorescence, circular dichroism and Raman spectroscopy
Biochim. Biophys. Acta
1161
303-310
1993
Bos taurus
brenda
Atack, J.R.; Rapoport, S.I.; Varley, C.L.;
Characterization of inositol monophosphatase in human cerebrospinal fluid
Brain Res.
613
305-308
1993
Homo sapiens
brenda
Kwon, H.Y.; Lim, B.H.; Park, H.S.; Lee, Y.L.; Lee, E.H.; Choi, S.Y.; Park, H.J.
Rat duodenal mucosa inositol monophosphatase; novel enzyme of which properties are distinct from brain enzyme
J. Biochem. Mol. Biol.
31
274-280
1998
Rattus norvegicus
-
brenda
Kwon, H.Y.; Shin, H.C.; Lee, Y.L.; Park, H.J.; Cho, S.W.; Choi, S.Y.
Purification and properties of myo-inositol monophosphate phosphatase from porcine brain
Mol. Cells
3
95-99
1993
Sus scrofa
-
brenda
Vadnal, R.E.; Parthasarathy, R.; Parthasarathy, L.; Ramesh, T.G.; Shyamaladevi, C.S.
The identification of a membrane-bound myo-inositol 1-phosphatase in rat brain, liver, and testes
Biochem. Int.
26
935-941
1992
Rattus norvegicus
brenda
Parthasarathy, L.; Vadnal, R.E.; Parthasarathy, R.; Shyamaldevi, C.S.
Minireview. Biochemical and molecular properties of lithium-sensitive myo-inositol monophosphatase
Life Sci.
54
1127-1142
1994
Bos taurus, Homo sapiens, Lilium longiflorum, Rattus norvegicus
brenda
Wang, X.L.; Akhtar, R.A.; Abdel-Latif, A.A.
Studies on the properties of myo-inositol-1,4,5-trisphosphate 5-phosphatase and myo-inositol monophosphatase in bovine iris sphincter smooth muscle: effects of okadaic acid and protein phosphorylation
Biochim. Biophys. Acta
1222
27-36
1994
Bos taurus
brenda
Janczarek, M.; Skorupska, A.
The Rhizobium leguminosarum bv. trifolii pssB gene product is an inositol monophosphatase that influences exopolysaccharide synthesis
Arch. Microbiol.
175
143-151
2001
Rhizobium leguminosarum
brenda
Navarro-Avino, J.P.; Belles, J.M.; Serrano, R.
Yeast inositol mono- and trisphosphate levels are modulated by inositol monophosphatase activity and nutrients
Biochem. Biophys. Res. Commun.
302
41-45
2003
Saccharomyces cerevisiae
brenda
Nigou, J.; Besra, G.S.
Characterization and regulation of inositol monophosphatase activity in Mycobacterium smegmatis
Biochem. J.
361
385-390
2002
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155
brenda
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
brenda
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)
brenda
Nigou, J.; Dover, L.G.; Besra, G.S.
Purification and biochemical characterization of Mycobacterium tuberculosis SuhB, an inositol monophosphatase involved in inositol biosynthesis
Biochemistry
41
4392-4398
2002
Mycobacterium tuberculosis
brenda
Berggard, T.; Szczepankiewicz, O.; Thulin, E.; Linse, S.
Myo-inositol monophosphatase is an activated target of calbindin D28k
J. Biol. Chem.
277
41954-41959
2002
Bos taurus
brenda
Fauroux, C.M.J.; Lee, M.; Cullis, P.M.; Douglas, K.T.; Gore, M.G.; Freeman, S.
Stereochemistry at phosphorus of the reaction catalyzed by myo-inositol monophosphatase
J. Med. Chem.
45
1363-1373
2002
Bos taurus
brenda
Bahn, J.H.; Kim, A.Y.; Jang, S.H.; Lee, B.R.; Ahn, J.Y.; Joo, H.M.; Kang, T.C.; Won, M.H.; Kwon, H.Y.; Kang, J.H.; Kwon, O.S.; Kim, H.B.; Cho, S.W.; Lee, K.S.; Park, J.; Choi, S.Y.
Production of monoclonal antibodies and immunohistochemical studies of brain myo-inositol monophosphate phosphatase
Mol. Cell
13
21-27
2002
Sus scrofa
brenda
Murray, M.; Greenberg, M.L.
Expression of yeast INM1 encoding inositol monophosphatase is regulated by inositol, carbon source and growth stage and is decreased by lithium and valproate
Mol. Microbiol.
36
651-661
2000
Saccharomyces cerevisiae
brenda
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
brenda
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, Methanocaldococcus jannaschii, Methanocaldococcus jannaschii MJ0109, Archaeoglobus fulgidus AF2372
brenda
Gill, R.; Mohammed, F.; Badyal, R.; Coates, L.; Erskine, P.; Thompson, D.; Cooper, J.; Gore, M.; Wood, S.
High-resolution structure of myo-inositol monophosphatase, the putative target of lithium therapy
Acta Crystallogr. Sect. D
61
545-555
2005
Bos taurus (P20456), Bos taurus
brenda
Gu, X.; Chen, M.; Shen, H.; Jiang, X.; Huang, Y.; Wang, H.
Rv2131c gene product: an unconventional enzyme that is both inositol monophosphatase and fructose-1,6-bisphosphatase
Biochem. Biophys. Res. Commun.
339
897-904
2006
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
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
Methanocaldococcus jannaschii, Thermotoga maritima, Archaeoglobus fulgidus (O30298), Archaeoglobus fulgidus
brenda
Morgan, A.J.; Wang, Y.K.; Roberts, M.F.; Miller, S.J.
Chemistry and biology of deoxy-myo-inositol phosphates: stereospecificity of substrate interactions within an archaeal and a bacterial IMPase
J. Am. Chem. Soc.
126
15370-15371
2004
Archaeoglobus fulgidus, Escherichia coli
brenda
Kim, D.W.; Hong, J.W.; Eum, W.S.; Choi, H.S.; Choi, S.H.; Kim, S.Y.; Lee, B.R.; An, J.J.; Lee, S.H.; Lee, S.R.; Kwon, O.S.; Kwon, H.Y.; Cho, S.W.; Lee, K.S.; Park, J.; Choi, S.Y.
Inactivation of brain myo-inositol monophosphate phosphatase by pyridoxal-5'-phosphate
J. Biochem. Mol. Biol.
38
58-64
2005
Sus scrofa
brenda
Zheng, W.; Brandish, P.E.; Kolodin, D.G.; Scolnick, E.M.; Strulovici, B.
High-throughput cell-based screening using scintillation proximity assay for the discovery of inositol phosphatase inhibitors
J. Biomol. Screen.
9
132-140
2004
Homo sapiens
brenda
Miller, D.J.; Bashir-Uddin Surfraz, M.; Akhtar, M.; Gani, D.; Allemann, R.K.
Removal of the phosphate group in mechanism-based inhibitors of inositol monophosphatase leads to unusual inhibitory activity
Org. Biomol. Chem.
2
671-688
2004
Bos taurus
brenda
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
brenda
Islas-Flores, I.; Villanueva, M.A.
Inositol-1 (or 4)-monophosphatase from Glycine max embryo axes is a phosphatase with broad substrate specificity that includes phytate dephosphorylation
Biochim. Biophys. Acta
1770
543-550
2007
Glycine max
brenda
Caselli, A.; Casolaro, M.; Ranaldi, F.; Manao, G.; Camici, G.; Giachetti, E.
Kinetic mechanism of the Zn-dependent aryl-phosphatase activity of myo-inositol-1-phosphatase
Biophys. Chem.
125
435-443
2007
Bos taurus
brenda
Brown, A.K.; Meng, G.; Ghadbane, H.; Scott, D.J.; Dover, L.G.; Nigou, J.; Besra, G.S.; Fuetterer, K.
Dimerization of inositol monophosphatase Mycobacterium tuberculosis SuhB is not constitutive, but induced by binding of the activator Mg2+
BMC Struct. Biol.
7
55
2007
Mycobacterium tuberculosis
brenda
Stieglitz, K.A.; Roberts, M.F.; Li, W.; Stec, B.
Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima
FEBS J.
274
2461-2469
2007
Thermotoga maritima (O33832), Thermotoga maritima
brenda
Tanizawa, Y.; Kuhara, A.; Inada, H.; Kodama, E.; Mizuno, T.; Mori, I.
Inositol monophosphatase regulates localization of synaptic components and behavior in the mature nervous system of C. elegans
Genes Dev.
20
3296-3310
2006
Caenorhabditis elegans
brenda
Wang, Y.; Stieglitz, K.A.; Bubunenko, M.; Court, D.L.; Stec, B.; Roberts, M.F.
The structure of the R184A mutant of the inositol monophosphatase encoded by suhB and implications for its functional interactions in Escherichia coli
J. Biol. Chem.
282
26989-26996
2007
Escherichia coli (P0ADG4), Escherichia coli
brenda
Ohnishi, T.; Ohba, H.; Seo, K.C.; Im, J.; Sato, Y.; Iwayama, Y.; Furuichi, T.; Chung, S.K.; Yoshikawa, T.
Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1
J. Biol. Chem.
282
637-646
2007
Mus musculus (O55023), Mus musculus (Q91UZ5)
brenda
Miller, D.J.; Allemann, R.K.
myo-inositol monophosphatase: a challenging target for mood stabilising drugs
Mini Rev. Med. Chem.
7
107-113
2007
Homo sapiens
brenda
Patra, B.; Ghosh Dastidar, K.; Maitra, S.; Bhattacharyya, J.; Majumder, A.L.
Functional identification of sll1383 from Synechocystis sp PCC 6803 as L-myo-inositol 1-phosphate phosphatase (EC 3.1.3.25): molecular cloning, expression and characterization
Planta
225
1547-1558
2007
Synechocystis sp.
brenda
Arai, R.; Ito, K.; Ohnishi, T.; Ohba, H.; Akasaka, R.; Bessho, Y.; Hanawa-Suetsugu, K.; Yoshikawa, T.; Shirouzu, M.; Yokoyama, S.
Crystal structure of human myo-inositol monophosphatase 2, the product of the putative susceptibility gene for bipolar disorder, schizophrenia, and febrile seizures
Proteins
67
732-742
2007
Homo sapiens
brenda
Fu, J.; Peterson, K.; Guttieri, M.; Souza, E.; Raboy, V.
Barley (Hordeum vulgare L.) inositol monophosphatase: gene structure and enzyme characteristics
Plant Mol. Biol.
67
629-642
2008
Hordeum vulgare (B3DFH0), Hordeum vulgare
brenda
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (Q6NPM8), Arabidopsis thaliana (Q94F00), Arabidopsis thaliana (Q9M8S8)
brenda
Kalujnaia, S.; Cramb, G.
Regulation of expression of the myo-inositol monophosphatase 1 gene in osmoregulatory tissues of the European eel Anguilla anguilla after seawater acclimation
Ann. N. Y. Acad. Sci.
1163
433-436
2009
Anguilla anguilla
brenda
Andreassi, C.; Zimmermann, C.; Mitter, R.; Fusco, S.; Devita, S.; Saiardi, A.; Riccio, A.
An NGF-responsive element targets myo-inositol monophosphatase-1 mRNA to sympathetic neuron axons
Nat. Neurosci.
13
291-301
2010
Rattus norvegicus (P97697)
brenda
Bhattacharyya, S.; Dutta, D.; Ghosh, A.K.; Das, A.K.
Cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of an inositol monophosphatase family protein (SAS2203) from Staphylococcus aureus MSSA476
Acta Crystallogr. Sect. F
67
471-474
2011
Staphylococcus aureus (A0A1I9GET0), Staphylococcus aureus MSSA476 (A0A1I9GET0), Staphylococcus aureus MSSA476
brenda
Movahedzadeh, F.; Wheeler, P.R.; Dinadayala, P.; Av-Gay, Y.; Parish, T.; Daffe, M.; Stoker, N.G.
Inositol monophosphate phosphatase genes of Mycobacterium tuberculosis
BMC Microbiol.
10
50
2010
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, ATCC 25618
brenda
Kalujnaia, S.; McVee, J.; Kasciukovic, T.; Stewart, A.J.; Cramb, G.
A role for inositol monophosphatase 1 (IMPA1) in salinity adaptation in the euryhaline eel (Anguilla anguilla)
FASEB J.
24
3981-3991
2010
Anguilla anguilla
brenda
Fujita, S.; Ohnishi, T.; Okuda, S.; Kobayashi, R.; Fukuno, S.; Furuta, D.; Kikuchi, T.; Yoshikawa, T.; Fujita, N.
In silico study on the substrate binding manner in human myo-inositol monophosphatase 2
J. Mol. Model.
17
2559-2567
2011
Homo sapiens
brenda
Sato, Y.; Yazawa, K.; Yoshida, S.; Tamaoki, M.; Nakajima, N.; Iwai, H.; Ishii, T.; Satoh, S.
Expression and functions of myo-inositol monophosphatase family genes in seed development of Arabidopsis
J. Plant Res.
124
385-394
2011
Arabidopsis thaliana (Q6NPM8), Arabidopsis thaliana (Q94F00), Arabidopsis thaliana (Q9M8S8)
brenda
Li, Z.; Stieglitz, K.; Shrout, A.; Wei, Y.; Weis, R.; Stec, B.; Roberts, M.
Mobile loop mutations in an archaeal inositol monophosphatase: Modulating three-metal ion assisted catalysis and lithium inhibition
Protein Sci.
19
309-318
2010
Methanocaldococcus jannaschii
brenda
Stieglitz, K.A.; Johnson, K.A.; Yang, H.; Roberts, M.F.; Seaton, B.A.; Head, J.F.; Stec, B.
Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop
J. Biol. Chem.
277
22863-22874
2002
Archaeoglobus fulgidus (O30298), Archaeoglobus fulgidus
brenda
Singh, N.; Halliday, A.C.; Knight, M.; Lack, N.A.; Lowe, E.; Churchill, G.C.
Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens
Acta Crystallogr. Sect. F
68
1149-1152
2012
Mus musculus (O55023), Mus musculus, Homo sapiens (P29218), Homo sapiens
brenda
Wang, F.K.; Latifi, A.; Chen, W.L.; Zhang, C.C.
The inositol monophosphatase All2917 (IMPA1) is involved in osmotic adaptation in Anabaena sp. PCC7120
Environ. Microbiol. Rep.
4
622-632
2012
Anabaena sp., Anabaena sp. PCC 7120
brenda
Dutta, A.; Bhattacharyya, S.; Dutta, D.; Das, A.K.
Structural elucidation of the binding site and mode of inhibition of Li+ and Mg2+ in inositol monophosphatase
FEBS J.
281
5309-5324
2014
Staphylococcus aureus (A0A1I9GET0), Staphylococcus aureus MSSA476 (A0A1I9GET0)
brenda
Kimata, T.; Tanizawa, Y.; Can, Y.; Ikeda, S.; Kuhara, A.; Mori, I.
Synaptic polarity depends on phosphatidylinositol signaling regulated by myo-inositol monophosphatase in Caenorhabditis elegans
Genetics
191
509-521
2012
Caenorhabditis elegans
brenda
Haimovich, A.; Eliav, U.; Goldbourt, A.
Determination of the lithium binding site in inositol monophosphatase, the putative target for lithium therapy, by magic-angle-spinning solid-state NMR
J. Am. Chem. Soc.
134
5647-5651
2012
Escherichia coli
brenda
Lu, S.; Huang, W.; Li, X.; Huang, Z.; Liu, X.; Chen, Y.; Shi, T.; Zhang, J.
Insights into the role of magnesium triad in myo-inositol monophosphatase: metal mechanism, substrate binding, and lithium therapy
J. Chem. Inf. Model.
52
2398-2409
2012
Bos taurus (P20456)
brenda
Wang, X.; Hirao, H.
ONIOM (DFT:MM) study of the catalytic mechanism of myo-inositol monophosphatase: essential role of water in enzyme catalysis in the two-metal mechanism
J. Phys. Chem. B
117
833-842
2013
Bos taurus (P20456)
brenda
Lu, Y.; Wang, L.; Teng, F.; Zhang, J.; Hu, M.; Tao, Y.
Production of myo-inositol from glucose by a novel trienzymatic cascade of polyphosphate glucokinase, inositol 1-phosphate synthase and inositol monophosphatase
Enzyme Microb. Technol.
112
1-5
2018
Escherichia coli
brenda
Goswami, R.; Bondoc, J.M.G.; Wheeler, P.R.; Jafari, A.; Gonzalez, T.; Mehboob, S.; Movahedzadeh, F.
Inositol monophosphatase A bifunctional enzyme in Mycobacterium smegmatis
ACS Omega
3
13876-13881
2018
Mycolicibacterium smegmatis (A0QX86), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0QX86)
brenda
Kraft, L.; Roe, S.M.; Gill, R.; Atack, J.R.
Co-crystallization of human inositol monophosphatase with the lithium mimetic L-690,330
Acta Crystallogr. Sect. D
74
973-978
2018
Homo sapiens (P29218), Homo sapiens
brenda
Murry, R.; Kniemeyer, O.; Krause, K.; Saiardi, A.; Kothe, E.
Crosstalk between Ras and inositol phosphate signaling revealed by lithium action on inositol monophosphatase in Schizophyllum commune
Adv. Biol. Regul.
72
S2212
2019
Schizophyllum commune
brenda
Rafikov, R.; McBride, M.L.; Zemskova, M.; Kurdyukov, S.; McClain, N.; Niihori, M.; Langlais, P.R.; Rafikova, O.
Inositol monophosphatase 1 as a novel interacting partner of RAGE in pulmonary hypertension
Am. J. Physiol. Lung Cell Mol. Physiol.
316
L428-L444
2019
Rattus norvegicus (P97697)
brenda
Nourbakhsh, A.; Collakova, E.; Gillaspy, G.
Characterization of the inositol monophosphatase gene family in Arabidopsis
Front. Plant Sci.
5
725
2015
Arabidopsis thaliana (Q94F00)
brenda
Ruszkowski, M.; Dauter, Z.
Structural studies of Medicago truncatula histidinol phosphate phosphatase from inositol monophosphatase superfamily reveal details of penultimate step of histidine biosynthesis in plants
J. Biol. Chem.
291
9960-9973
2016
Medicago truncatula (G7J7Q5), Medicago truncatula
brenda
Nakatsu, F.; Messa, M.; Nandez, R.; Czapla, H.; Zou, Y.; Strittmatter, S.M.; De Camilli, P.
Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic pathway
J. Cell Biol.
209
85-95
2015
Mus musculus (Q8CDA1)
brenda
Agam, G.; Almog, O.
Calbindin D28k and S100B have a similar interaction site with the lithium-inhibitable enzyme inositol monophosphatase-1 a new drug target site
J. Med. Chem.
58
2042-2044
2015
Homo sapiens (P05937)
brenda
Figueiredo, T.; Melo, U.S.; Pessoa, A.L.; Nobrega, P.R.; Kitajima, J.P.; Rusch, H.; Vaz, F.; Lucato, L.T.; Zatz, M.; Kok, F.; Santos, S.
A homozygous loss-of-function mutation in inositol monophosphatase 1 (IMPA1) causes severe intellectual disability
Mol. Psychiatry
21
1125-1129
2016
Homo sapiens (P29218), Homo sapiens
brenda
Ferruz, N.; Tresadern, G.; Pineda-Lucena, A.; De Fabritiis, G.
Multibody cofactor and substrate molecular recognition in the myo-inositol monophosphatase enzyme
Sci. Rep.
6
30275
2016
Homo sapiens (P29218)
brenda