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Information on EC 3.1.3.62 - multiple inositol-polyphosphate phosphatase
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3.1.3.62 multiple inositol-polyphosphate phosphataseIUBMB Comments
This enzyme exists in two isoforms. It also acts on Ins(1,3,4,5)P4 to yield Ins(1,4,5)P3.
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Word Map
- 3.1.3.62
-
kallikrein-related
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kallikreins
-
prostate-specific
- 1,3,4-trisphosphate
- pentakisphosphate
- 1,3,4,5,6-pentakisphosphate
-
pro-hgf
-
activator-inhibitor
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
(HSA)MINPP1, (MMU)Minpp1, 1D-myo-inositol-1,3,4,5-tetrakisphosphate 3-phosphohydrolase, alkaline phytase isoform 1, alkaline phytase isoform 2, HvPhyIIa1, HvPhyIIa2, HvPhyIIb, inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase, inositol 1,3,4,5-tetrakisphosphate 3-phosphomonoesterase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1D-myo-inositol-1,3,4,5-tetrakisphosphate 3-phosphohydrolase
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-
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inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase
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inositol 1,3,4,5-tetrakisphosphate 3-phosphomonoesterase
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inositol 1,3,4,5-tetrakisphosphate-5-phosphomonoesterase
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inositol tetrakisphosphate phosphomonoesterase
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inositol-1,3,4,5-tetrakisphosphate 3-phosphatase
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Minpp
MIPP
multiple inositol polyphosphate phosphatase
phosphatase, inositol 1,3,4,5-tetrakisphosphate 3-
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additional information
Minpp
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MIPP
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multiple inositol polyphosphate phosphatase
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additional information
distinct group within the histidine phosphatase family
additional information
structural and functional relationship between MIPP and histidine acid phosphatase
additional information
distinct group within the histidine phosphatase family
additional information
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structural and functional relationship between MIPP and histidine acid phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate
formerly D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = D-myo-inositol 1,4,5-trisphosphate + phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
1D-myo-inositol-hexakisphosphate 5-phosphohydrolase
This enzyme exists in two isoforms. It also acts on Ins(1,3,4,5)P4 to yield Ins(1,4,5)P3.
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CAS REGISTRY NUMBER
COMMENTARY
116958-30-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-myo-inositol 1,2,3,4,5,6-hexakisphosphate + H2O
D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
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-
-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
inositol 3,4,5,6-tetrakisphosphate + H2O
?
-
about 10% of activity with inositol 1,3,4,5-tetrakisphosphate
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-
?
myo-inositol hexakisphosphate + H2O
myo-inositol pentakisphosphate + phosphate
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-
-
-
?
scyllo-inositol hexakisphosphate + H2O
scyllo-inositol pentakisphosphate + phosphate
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-
-
-
?
2,3-bisphosphoglycerate + H2O
2-phosphoglycerate + phosphate
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-
-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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recombinant N-terminal truncated cytosolic MIPP generates inositol 1,4,5-trisphosphate in an intact cell
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?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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enzyme may be regulated by the intracellular concentrations of inositol tris- and tetrakisphosphates
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?
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
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?
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
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-
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?
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
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?
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
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?
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
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-
-
?
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
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-
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-
?
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
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recombinant N-terminal truncated cytosolic MIPP
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?
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
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inositol pentakisphosphate and inositol hexakisphosphate are likely to be the preferred substrates in vivo
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?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
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?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
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?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
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?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
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?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
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?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
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at least 4 isomers: D- and/or L-inositol 1,2,4,5,6-pentakisphosphate, D-inositol 1,3,4,5,6-pentakisphosphate, D-inositol 1,2,3,4,6-pentakisphosphate and D- and/or L-inositol 1,2,3,4,5-pentakisphosphate
?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
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recombinant N-terminal truncated cytosolic MIPP
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-
?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
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inositol pentakisphosphate and inositol hexakisphosphate are likely to be the preferred substrates in vivo
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?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
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?
additional information
?
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catalytic requirement for the C-terminus and His-370 of MIPP
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additional information
?
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dephosphorylates inositol signaling molecules InsP5 and InsP6
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additional information
?
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Minpp is important to chondrocyte differentiation in a manner independent of inositol polyphosphate turnover
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additional information
?
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dephosphorylates inositol signaling molecules InsP5 and InsP6
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additional information
?
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dephosphorylates inositol signaling molecules InsP5 and InsP6
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additional information
?
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not: inositol 1,3,4-trisphosphate, inositol 1,3-bisphosphate, inositol 3,4-bisphosphate, 4-nitrophenyl phosphate
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additional information
?
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enzyme is relatively unimportant to inositol 1,3,4,5-tetrakisphosphate metabolism in vivo
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additional information
?
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MIPP mRNA is upregulated during chondrocyte hypertrophy, MIPP may aid bone mineralization and salvage the inositol moiety prior to apoptosis
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additional information
?
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inositol 1,3,4,5-tetrakisphosphate 3-phosphatase is unlikely to be an important activity in vivo
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additional information
?
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function is unrelated to the metabolism of Ca2+-mobilizing cellular signals
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additional information
?
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role in the metabolism of inositol phosphates, but probably no important participant in signal transduction
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,4,5-trisphosphate + phosphate
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enzyme may be regulated by the intracellular concentrations of inositol tris- and tetrakisphosphates
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?
inositol 1,3,4,5,6-pentakisphosphate + H2O
inositol 1,4,5,6-tetrakisphosphate + phosphate
-
inositol pentakisphosphate and inositol hexakisphosphate are likely to be the preferred substrates in vivo
-
?
inositol hexakisphosphate + H2O
inositol pentakisphosphate + phosphate
-
inositol pentakisphosphate and inositol hexakisphosphate are likely to be the preferred substrates in vivo
-
?
additional information
?
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Minpp is important to chondrocyte differentiation in a manner independent of inositol polyphosphate turnover
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additional information
?
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enzyme is relatively unimportant to inositol 1,3,4,5-tetrakisphosphate metabolism in vivo
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-
-
additional information
?
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MIPP mRNA is upregulated during chondrocyte hypertrophy, MIPP may aid bone mineralization and salvage the inositol moiety prior to apoptosis
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-
additional information
?
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inositol 1,3,4,5-tetrakisphosphate 3-phosphatase is unlikely to be an important activity in vivo
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-
additional information
?
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function is unrelated to the metabolism of Ca2+-mobilizing cellular signals
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-
additional information
?
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role in the metabolism of inositol phosphates, but probably no important participant in signal transduction
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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
Mg2+
-
2.5fold activation at 5-10 mM, no activation at 1 mM and physiologically relevant concentrations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ammonium phosphate buffer
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1 to 10 mM activates, higher concentrations are inhibitory
Endogenous heat-stable inhibitor
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from soluble and particulate regions of liver cells
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Inositol 1,3,4,5,6-pentakisphosphate
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0.001 mM, 50% inhibition; competitive; strong, kinetics
Inositol 1,3,4,5,6-pentakisphosphate
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competitive; strong, kinetics; turkey hemoglobin reverses
inositol 3,4,5,6-tetrakisphosphate
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commercially available with 12% inositol 2,4,5,6-tetrakisphosphate, from turkey erythrocytes, marked inhibition, linear mixed-type inhibition
Inositol hexakisphosphate
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mixed inhibitor, 0.001 mM, 85% inhibition; more effective than inositol pentakisphosphate; strong, kinetics
Inositol hexakisphosphate
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competitive, turkey hemoglobin reverses; more effective than inositol pentakisphosphate; strong, kinetics
Inositol hexakisphosphate
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more effective than inositol pentakisphosphate; strong, kinetics
additional information
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extracts of liver, heart, kidney, testis and brain contain different amounts of endogenous inhibitors of enzyme activity
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additional information
-
not inhibited by Mg2+, Ca2+, Li+, non-hydrolysable adenine, guanine nucleotides or deoxynucleotides
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ammonium phosphate buffer
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1 to 10 mM activates, higher concentrations are inhibitory
hemoglobin
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from turkey, activates by removing the inhibitors inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Colonic Neoplasms
Ataxin-10 is part of a cachexokine cocktail triggering cardiac metabolic dysfunction in cancer cachexia.
Neoplasms
Multiple inositol polyphosphate phosphatase: evolution as a distinct group within the histidine phosphatase family and chromosomal localization of the human and mouse genes to chromosomes 10q23 and 19.
Neoplasms
Tumour cells can employ extracellular Ins(1,2,3,4,5,6)P(6) and multiple inositol-polyphosphate phosphatase 1 (MINPP1) dephosphorylation to improve their proliferation.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic data of the cytosolic enzyme
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0.007 - 0.008
D-myo-Inositol 1,3,4,5-tetrakisphosphate
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pH 7.2, 37°C, cytosolic enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity of MINPP towards other phosphates, relative to inositol hexakisphosphate, is as follows: p-nitrophenyl phosphate: 17%, ATP: 11%, D-ribose 1-phosphate: 0.31%; Q78A mutant shows differences in its specificity profile compared to wild-type enzyme: relative to inositol hexakisphosphate, the activity towards other phosphates are as follows: p-nitrophenyl phosphate: 7%, ATP: 12%, D-ribose 1-phosphate: 3%
additional information
expression of HvPhyIIb in Escherichia coli reveals that the MINPPs possesses a significant phytase activity with narrow substrate specificity for phytate
additional information
expression of HvPhyIIb in Escherichia coli reveals that the MINPPs possesses a significant phytase activity with narrow substrate specificity for phytate
additional information
expression of HvPhyIIb in Escherichia coli reveals that the MINPPs possesses a significant phytase activity with narrow substrate specificity for phytate
additional information
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expression of HvPhyIIb in Escherichia coli reveals that the MINPPs possesses a significant phytase activity with narrow substrate specificity for phytate
additional information
expression of TaPhyIIa2 in Escherichia coli reveals that the MINPPs possesses a significant phytase activity with narrow substrate specificity for phytate
additional information
expression of TaPhyIIa2 in Escherichia coli reveals that the MINPPs possesses a significant phytase activity with narrow substrate specificity for phytate
additional information
expression of TaPhyIIa2 in Escherichia coli reveals that the MINPPs possesses a significant phytase activity with narrow substrate specificity for phytate
additional information
expression of TaPhyIIa2 in Escherichia coli reveals that the MINPPs possesses a significant phytase activity with narrow substrate specificity for phytate
additional information
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expression of TaPhyIIa2 in Escherichia coli reveals that the MINPPs possesses a significant phytase activity with narrow substrate specificity for phytate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5 - 9
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plateau within the range, inositol 1,3,4,5,6-pentakisphosphate or inositol hexakisphosphate as substrate, in absence of Mg2+
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
65
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
chondrocyte progenitor cell line, developmentally specific changes in MINPP expression
brenda
additional information
-
nonsynchronous primary cultures of growth plate chondrocytes from rib cartilage, developmentally specific changes in MINPP expression
brenda
additional information
not expressed in peripheral blood leukocytes
brenda
additional information
cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination
brenda
additional information
cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination
brenda
additional information
cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination
brenda
additional information
-
cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination
brenda
additional information
cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination
brenda
additional information
cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination
brenda
additional information
cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination
brenda
additional information
cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination
brenda
additional information
-
cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination; cDNAs show significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb, the cDNAs are present during late seed development and germination
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant N-terminal truncated form lacking the ER signal peptide is cytosolic
brenda
-
recombinant Minpp expressed in murine ATDC-5 cells, only expressed inside the ER
brenda
ER-based protein, N-terminal ER-targeting domain
brenda
all cDNAs contain an N-terminal signal peptide encoding sequence, and a KDEL-like sequence, KTEL, is present at the C-terminal, indicating that the enzyme is targeted to and retained within the endoplasmic reticulum; all cDNAs contain an N-terminal signal peptide encoding sequence, and a KDEL-like sequence, KTEL, is present at the C-terminal, indicating that the enzyme is targeted to and retained within the endoplasmic reticulum; all cDNAs contain an N-terminal signal peptide encoding sequence, and a KDEL-like sequence, KTEL, is present at the C-terminal, indicating that the enzyme is targeted to and retained within the endoplasmic reticulum
brenda
-
liver enzyme, inside, approximately evenly distributed between the rough and smooth subfractions
brenda
-
largely endoplasmic reticulum-confined MIPP
brenda
-
ER-based protein, N-terminal ER-targeting domain
brenda
all cDNAs contain an N-terminal signal peptide encoding sequence, and a KDEL-like sequence, KTEL, is present at the C-terminal, indicating that the enzyme is targeted to and retained within the endoplasmic reticulum; all cDNAs contain an N-terminal signal peptide encoding sequence, and a KDEL-like sequence, KTEL, is present at the C-terminal, indicating that the enzyme is targeted to and retained within the endoplasmic reticulum; all cDNAs contain an N-terminal signal peptide encoding sequence, and a KDEL-like sequence, KTEL, is present at the C-terminal, indicating that the enzyme is targeted to and retained within the endoplasmic reticulum; all cDNAs contain an N-terminal signal peptide encoding sequence, and a KDEL-like sequence, KTEL, is present at the C-terminal, indicating that the enzyme is targeted to and retained within the endoplasmic reticulum
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
B0EQX5_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
448
0
52262
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
51000
x * 51000, recombinant MIPP expressed in Escherichia coli M15, SDS-PAGE and Western blot analysis
53400
x * 53400, recombinant MIPP expressed in Escherichia coli M15, amino acid sequence analysis
54500
x * 54500, inclusive the putative signal sequence, amino acid sequence analysis
55000
55100
x * 55100, inclusive the putative signal sequence, amino acid sequence analysis
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
x * 51000, recombinant MIPP expressed in Escherichia coli M15, SDS-PAGE and Western blot analysis; x * 53400, recombinant MIPP expressed in Escherichia coli M15, amino acid sequence analysis
?
x * 55100, inclusive the putative signal sequence, amino acid sequence analysis
?
x * 54500, inclusive the putative signal sequence, amino acid sequence analysis
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q78A
-
Km: 0.06 (myo-inositol hexakisphosphate). Q78A mutant shows differences in its specificity profile compared to wild-type enzyme: relative to inositol hexakisphosphate, the activity towards other organic phosphates are as follows: p-nitrophenyl phosphate: 7%, ATP: 12%, ribose 1-phosphate: 3%
H89A
-
catalytically compromised mutant of MIPP1 that shows only 1% of the 2,3-diphosphoglycerate phosphatase activity of the wild type enzyme
additional information
additional information
L1ALP contains the histidine phosphatase conserved sequence, -RHGXRXP-, and therefore belongs to the histidine phosphatase family of enzymes unlike alkaline phytases from bacteria; L1ALP contains the histidine phosphatase conserved sequence, -RHGXRXP-, and therefore belongs to the histidine phosphatase family of enzymes unlike alkaline phytases from bacteria; two isoforms of alkaline phytase cDNAs, L1Alp1 and L1Alp2, which are 1467 and 1533 bp long and encode proteins of 487 and 511 amino acids, respectively, are identified. Phylogenetic analysis reveals that LlALP is most closely related to multiple inositol polyphosphate phosphatase (MINPP) from humans (25%) and rats (23%); two isoforms of alkaline phytase cDNAs, L1Alp1 and L1Alp2, which are 1467 and 1533 bp long and encode proteins of 487 and 511 amino acids, respectively, are identified. Phylogenetic analysis reveals that LlALP is most closely related to multiple inositol polyphosphate phosphatase (MINPP) from humans (25%) and rats (23%)
additional information
L1ALP contains the histidine phosphatase conserved sequence, -RHGXRXP-, and therefore belongs to the histidine phosphatase family of enzymes unlike alkaline phytases from bacteria; L1ALP contains the histidine phosphatase conserved sequence, -RHGXRXP-, and therefore belongs to the histidine phosphatase family of enzymes unlike alkaline phytases from bacteria; two isoforms of alkaline phytase cDNAs, L1Alp1 and L1Alp2, which are 1467 and 1533 bp long and encode proteins of 487 and 511 amino acids, respectively, are identified. Phylogenetic analysis reveals that LlALP is most closely related to multiple inositol polyphosphate phosphatase (MINPP) from humans (25%) and rats (23%); two isoforms of alkaline phytase cDNAs, L1Alp1 and L1Alp2, which are 1467 and 1533 bp long and encode proteins of 487 and 511 amino acids, respectively, are identified. Phylogenetic analysis reveals that LlALP is most closely related to multiple inositol polyphosphate phosphatase (MINPP) from humans (25%) and rats (23%)
additional information
-
mutant with active site histidine altered to alanine has abolished enzyme activity
additional information
mutant with active site histidine altered to alanine has abolished enzyme activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.4
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 37
4 - 37
-
MIPP1 is active at 4°C, albeit considerably less active than at 37°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20% v/v glycerol, 1 mg/ml bovine serum albumin, up to 12 months, stable
-
0°C, 10 mM Tris-HCl, pH 7.4, 100 mM KCl, 1 mM dithiothreitol, up to 1 month, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-Sepharose column chromatography
partial
recombinant (MMU)Minpp1 fusion protein expressed in Escherichia coli JM109
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding residues 19-445 of avian MINPP or residues 31-483 of human MINPP lacking the N-terminal ER targeting sequences and the C-terminal ER retention signals are amplified by PCR and cloned into pGEM Tvector and transformed into Escherichia coli
-
full-length Minpp cDNA is cloned and stably overexpressed in murine ATDC-5 cells at 2fold higher levels than in wild-type ATDC-5 cells, cellular effects of overexpression
-
MIPP cDNA from Jurkat T-cells is cloned and expressed in Escherichia coli M15 without the ER-targeting domain, full-length sequence
MIPP cDNA from liver and kidney is cloned and expressed in Escherichia coli M15, full-length sequence
-
N-terminal truncated cytosolic MIPP is expressed in the beta-cell line HIT M2.2.2, expression increases the basal Ca2+-concentration to a more normal level
-
sequenced and expressed in Escherichia coli JM109, located on chromosome 19, genomic organization
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
recombinant avian MINPP (0.7 micromol/mg protein/min) is the most active phytase found to date in any animal cell
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hughes, P.J.; Shears, S.B.
Inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate inhibit inositol-1,3,4,5-tetrakisphosphate 3-phosphatase in rat parotid glands
J. Biol. Chem.
265
9869-9875
1990
Rattus norvegicus
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Höer, A.; Oberdisse, E.
Inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate are inhibitors of the soluble inositol 1,3,4,5-tetrakisphosphate 3-phosphatase and the inositol 1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase from pig brain
Biochem. J.
278
219-224
1991
Sus scrofa
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Cullen, P.J.; Irvine, R.F.; Drobak, B.K.; Dawson, A.P.
Inositol 1,3,4,5-tetrakisphosphate causes release of Ca2+ from permeabilized mouse lymphoma L1210 cells by its conversion into inositol 1,4,5-trisphosphate
Biochem. J.
259
931-933
1989
Mus musculus
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Höer, A.; Höer, D.; Oberdisse, E.
Properties of a soluble inositol 1,3,4,5-tetrakisphosphate 3-phosphatase from porcine brain
Biochem. J.
270
715-719
1990
Sus scrofa
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Hodgson, M.E.; Shears, S.B.
Rat liver contains a potent endogenous inhibitor of inositol 1,3,4,5-tetrakisphosphate 3-phosphatase
Biochem. J.
267
831-834
1990
Rattus norvegicus
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Nogimori, K.; Hughes, P.J.; Glennon, M.C.; Hodgson, M.E.; Putney, J.W.; Shears, S.B.
Purification of an inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase activity from rat liver and the evaluation of its substrate specificity
J. Biol. Chem.
266
16499-16506
1991
Rattus norvegicus
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Van Dijken, P.; Lammers, A.A.; Van Haastert, P.J.M.
In Dictyostelium discoideum inositol 1,3,4,5-tetrakisphosphate is dephosphorylated by a 3-phosphatase and a 1-phosphatase
Biochem. J.
308
127-130
1995
Dictyostelium discoideum
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Craxton, A.; Ali, N.; Shears, S.B.
Comparison of the activities of a multiple inositol polyphosphate phosphatase obtained from several sources: a search for heterogeneity in this enzyme
Biochem. J.
305
491-498
1995
Meleagris gallopavo, Rattus norvegicus
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Hidaka, K.; Kanematsu, T.; Caffrey, J.J.; Takeuchi, H.; Shears, S.B.; Hirata, M.
The importance to chondrocyte differentiation of changes in expression of the multiple inositol polyphosphate phosphatase
Exp. Cell Res.
290
254-264
2003
Homo sapiens, Mus musculus, Oryctolagus cuniculus
brenda
Yu, J.; Leibiger, B.; Yang, S.N.; Caffery, J.J.; Shears, S.B.; Leibiger, I.B.; Barker, C.J.; Berggren, P.O.
Cytosolic multiple inositol polyphosphate phosphatase in the regulation of cytoplasmic free Ca2+ concentration
J. Biol. Chem.
278
46210-46218
2003
Rattus norvegicus
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Caffrey, J.J.; Hidaka, K.; Matsuda, M.; Hirata, M.; Shears, S.B.
The human and rat forms of multiple inositol polyphosphate phosphatase: functional homology with a histidine acid phosphatase up-regulated during endochondral ossification
FEBS Lett.
442
99-104
1999
Homo sapiens (Q9UNW1), Rattus norvegicus
brenda
Chi, H.; Tiller, G.E.; Dasouki, M.J.; Romano, P.R.; Wang, J.; O'Keefe, R.J.; Puzas, J.E.; Rosier, R.N.; Reynolds, P.R.
Multiple inositol polyphosphate phosphatase: evolution as a distinct group within the histidine phosphatase family and chromosomal localization of the human and mouse genes to chromosomes 10q23 and 19
Genomics
56
324-336
1999
Homo sapiens, Homo sapiens (Q9UNW1), Mus musculus, Mus musculus (Q9Z2L6)
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Deleu, S.; Choi, K.; Pesesse, X.; Cho, J.; Sulis, M.L.; Parsons, R.; Shears, S.B.
Physiological levels of PTEN control the size of the cellular Ins(1,3,4,5,6)P5 pool
Cell. Signal.
18
488-498
2006
Homo sapiens
brenda
Cho, J.; Choi, K.; Darden, T.; Reynolds, P.R.; Petitte, J.N.; Shears, S.B.
Avian multiple inositol polyphosphate phosphatase is an active phytase that can be engineered to help ameliorate the planets 'phosphate crisis'
J. Biotechnol.
126
248-259
2006
Gallus gallus
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Mehta, B.D.; Jog, S.P.; Johnson, S.C.; Murthy, P.P.
Lily pollen alkaline phytase is a histidine phosphatase similar to mammalian multiple inositol polyphosphate phosphatase (MINPP)
Phytochemistry
67
1874-1886
2006
Lilium longiflorum (Q0GYS1), Lilium longiflorum (Q0GYS2)
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Dionisio, G.; Holm, P.B.; Brinch-Pedersen, H.
Wheat (Triticum aestivum L.) and barley (Hordeum vulgare L.) multiple inositol polyphosphate phosphatases (MINPPs) are phytases expressed during grain filling and germination
Plant Biotechnol. J.
5
325-338
2007
Hordeum vulgare (A0FHA7), Hordeum vulgare (A0FHA8), Hordeum vulgare (A0FHA9), Hordeum vulgare, Triticum aestivum (A0FHB0), Triticum aestivum (A0FHB1), Triticum aestivum (A0FHB2), Triticum aestivum (A0FHB3), Triticum aestivum
brenda
Cho, J.; King, J.S.; Qian, X.; Harwood, A.J.; Shears, S.B.
Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt
Proc. Natl. Acad. Sci. USA
105
5998-6003
2008
Dictyostelium discoideum, Homo sapiens, Rattus norvegicus
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