Information on EC 3.1.3.56 - inositol-polyphosphate 5-phosphatase

for references in articles please use BRENDA:EC3.1.3.56
Word Map on EC 3.1.3.56
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.3.56
-
RECOMMENDED NAME
GeneOntology No.
inositol-polyphosphate 5-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate
show the reaction diagram
D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1D-myo-inositol hexakisphosphate biosynthesis II (mammalian)
-
-
D-myo-inositol (1,3,4)-trisphosphate biosynthesis
-
-
D-myo-inositol (1,4,5)-trisphosphate degradation
-
-
Inositol phosphate metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
1D-myo-inositol-1,4,5-trisphosphate 5-phosphohydrolase
One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids.
CAS REGISTRY NUMBER
COMMENTARY hide
106283-14-1
-
9082-57-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
sequence of clone BVCT
SwissProt
Manually annotated by BRENDA team
type I enzyme
-
-
Manually annotated by BRENDA team
Frog
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
the increase in the levels of 1D-myo-inositol 1,4,5-trisphosphate/Ca2+ caused by deficiency of inositol polyphosphate 5-phosphatases is sufficient to break pollen dormancy and to trigger early germination
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
show the reaction diagram
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
show the reaction diagram
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate
show the reaction diagram
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
show the reaction diagram
1D-myo-inositol 1,2,3,4,5-pentakisphosphate + H2O
1D-myo-inositol 1,2,3,4-tetrakisphosphate + phosphate
show the reaction diagram
-
preferred substrate
-
-
?
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O
1D-myo-inositol 1,2,4,6-tetrakisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
1D-myo-inositol 1,2,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,2,4-trisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
show the reaction diagram
1D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O
1D-myo-inositol 1,4,6-trisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-disphosphate + phosphate
show the reaction diagram
-
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
1D-myo-inositol 2,4,5,6-tetrakisphosphate + H2O
1D-myo-inositol 2,4,6-trisphosphate + phosphate
show the reaction diagram
1D-myo-inositol 2,4,5-trisphosphate + H2O
1D-myo-inositol 2,4-bisphosphate + phosphate
show the reaction diagram
-
preferred substrate
-
-
?
1D-myo-inositol 3,4,5-trisphosphate + H2O
1D-myo-inositol 3,4-bisphosphate + phosphate
show the reaction diagram
-
-
-
?
1D-myo-inositol 3,5-bisphosphate + H2O
1D-myo-inositol 3-phosphate + phosphate
show the reaction diagram
-
-
-
?
1D-myo-inositol 4,5,6-trisphosphate + H2O
1D-myo-inositol 4,6-bisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
3-hydroxybenzene 1,2,4-trisphosphate + H2O
2,3-dihydroxybenzene 1,4-bisphosphate + phosphate
show the reaction diagram
-
this is the first example of its kind to illustrate that an unnatural aromatic polyphosphorylated molecule can be specifically dephosphorylated by type I Ins(1,4,5)P3 5-phosphatase. No reaction with benzene 1,2,4-trisphosphate
-
-
?
3-O-methylfluorescein phosphate + H2O
3-O-methylfluorescein + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
7-methyl-6-thioguanosine + H2O
7-methyl-6-thioguanine + ribose 1-phosphate
show the reaction diagram
-
spectrophotometric continous coupled enzyme assay substrate
-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
show the reaction diagram
D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O
D-myo-inositol 1,4,6-trisphosphate + phosphate
show the reaction diagram
-
poor substrate
-
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
glycerophosphoinositol 4,5-bisphosphate + H2O
glycerophosphoinositol 4-phosphate + phosphate
show the reaction diagram
-
at 13% of the rate of inositol 1,4,5-trisphosphate hydrolysis
-
?
inositol 1,2-cyclic 4,5-trisphosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
inositol 4,5-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphatidyl-L-myo-inositol 3,4,5-trisphosphate + H2O
phosphatidylinositol 3,4-bisphosphate + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-(3-sn-phosphatidyl)-L-myo-inositol 4,5-bisphosphate + H2O
phosphatidylinositol 4-phosphate + phosphate
show the reaction diagram
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
show the reaction diagram
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
1D-myo-inositol 1,4,5-trisphosphate + H2O
myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
-
-
-
-
?
1D-myo-inositol 3,4,5-trisphosphate + H2O
1D-myo-inositol 3,4-bisphosphate + phosphate
show the reaction diagram
O15357
-
-
-
?
1D-myo-inositol 3,5-bisphosphate + H2O
1D-myo-inositol 3-phosphate + phosphate
show the reaction diagram
O15357
-
-
-
?
D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
D-myo-inositol 1,3,4-trisphosphate + phosphate
show the reaction diagram
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
show the reaction diagram
inositol 4,5-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activates, competitive binding to other metal ions, KM 0.0145 mM and turnover number 7.28 s-1 at pH 7.0, 30C, recombinant enzyme
Ni2+
-
activates, competitive binding to other metal ions, KM 0.0064 mM and turnover number 5.48 s-1 at pH 7.0, 30C, recombinant enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
2,3-dihydroxybenzene 1,4-bisphosphate
-
-
3-benzyloxybenzene 1,2,4-trisphosphate
-
-
3-hydroxybenzene 1,2,4-trisphosphate
-
-
ammonium phosphate
-
-
AMP
-
slight inhibition
benzene 1,2,3,4-tetrakisphosphate
-
-
benzene 1,2,3,5-tetrakisphosphate
-
-
benzene 1,2,3-trisphosphate
-
-
benzene 1,2,4,5-tetrakisphosphate
-
-
benzene 1,2,4-trisphosphate
-
-
benzene 1,2-bisphosphate
-
-
benzene 1,3,5-trisphosphate
-
-
biphenyl 2,3',4,5',6-pentakisphosphate
-
-
CdCl2
D-6-deoxy-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
D-fructose 1,6-bisphosphate
D-fructose 2,6-bisphosphate
D-Glucose 1,6-bisphosphate
-
-
D-glucose 6-phosphate
Disulfiram
-
-
Glycerophosphoinositol 4,5-bisphosphate
-
competitive with D-myo-inositol 1,4,5-trisphosphate
Glycerophosphoinositol 4-phosphate
-
-
Inositol 1,3,4,5,6-pentakisphosphate
-
-
Inositol 1,3,4,5-tetrakisphosphate
inositol 1,4-bisphosphate
-
-
Inositol hexakisphosphate
-
competitive
L-chiro-Inositol 1,4,6-trisphosphorothioate
L-chiro-Inositol 2,3,5-trisphosphorothioate
L-myo-inositol 1,3,5-trisphosphorothioate
L-myo-inositol 1,4,5-trisphosphorothioate
N-ethylmaleimide
-
-
p-hydroxymercuribenzoate
Phenylglyoxal
-
Arg-343 and Arg-350 were found to be covalently modified; irreversible, substrates and 2,3-bisphosphoglycerate protect against inactivation
phosphate
-
-
protein PRIP-1
-
binding to PRIP-1, a Ins(1,4,5)P3-binding protein, inhibits the enzyme in vitro, in vivo binding of Ins(1,4,5)P3 to PRIP-1 prevents it from being hydrolyzed by the enzyme, PRIP-1 has a domain organization similar to phospholipase C-delta1, interaction analysis, overview
-
SDS
-
no activity with 0.1%
thimerosal
-
-
Triton X-100
-
20% of activity remaining with 1%
vanadate
Frog
-
30% inhibition at 1 mM
additional information
-
inositol 1,4-bisphosphate does not inhibit enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.056
7-methyl-6-thioguanosine
-
pH 7.0, 30C, recombinant enzyme
0.0008 - 0.019
D-myo-Inositol 1,3,4,5-tetrakisphosphate
0.001 - 0.32
D-myo-inositol 1,4,5-trisphosphate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
7-methyl-6-thioguanosine
-
pH 7.0, 30C, recombinant enzyme
340
D-myo-inositol 1,4,5-trisphosphate
-
37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
2,3-bisphosphoglycerate
-
-
0.07
Ca2+
-
-
0.02 - 0.035
Inositol 1,3,4,5,6-pentakisphosphate
0.0005 - 0.015
Inositol 1,3,4,5-tetrakisphosphate
0.01 - 0.015
Inositol hexakisphosphate
0.0000003
L-chiro-Inositol 1,4,6-trisphosphorothioate
-
-
0.00000023
L-chiro-Inositol 2,3,5-trisphosphorothioate
-
-
0.00000052
L-myo-inositol 1,3,5-trisphosphorothioate
-
-
0.00000043
L-myo-inositol 1,4,5-trisphosphorothioate
-
-
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021
2,3-dihydroxybenzene 1,4-bisphosphate
Homo sapiens
-
in the presence of 1 mM Ins-(1,4,5)P3 as substrate
0.068
3-benzyloxybenzene 1,2,4-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.021
3-hydroxybenzene 1,2,4-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.098
benzene 1,2,3,4-tetrakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate 6
0.078
benzene 1,2,3,5-tetrakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate 6
0.086
benzene 1,2,3-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.004
benzene 1,2,4,5-tetrakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.014
benzene 1,2,4-trisphosphate
0.016
benzene 1,3,5-trisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
0.001
biphenyl 2,3',4,5',6-pentakisphosphate
Homo sapiens
-
IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
additional information
benzene 1,2-bisphosphate
Homo sapiens
-
IC value is higher than 0.2 mM, IC50 value is obtained in the presence of 1 microM D-myo-inositol 1,4,5-trisphosphate as substrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0006
Frog
-
muscle, pH 7.2, 30C
0.0014
-
muscle and liver, pH 7.2, 30C
0.0028
-
Vmax, pH 7.0, 37C
0.003
-
main pulmonary artery, pH 7.2, 30C
0.0047
-
brain, pH 7.2, 30C
0.02
-
Vmax, membrane fraction, pH 7.2, 30C
0.089
recombinant enzyme from Escherichia coli
1.06
-
purified type I enzyme, pH 7.1, 30C
2.54
-
purified type I enzyme, pH 7.5, 37C
2.7
-
purified membrane associated enzyme, pH 7.2, 37C
3.2
-
measured in the presence of 0.05 mM of labeled Ins(1,4,5)P3
15.2
-
purified type II enzyme, pH 7.1, 30C
25.9
-
partially purified type I enzyme, 37C
31
-
Vmax, R343A mutant
175
-
purified membrane associated enzyme, pH 7.2, 37C
191
-
Vmax, native enzyme
237
-
Vmax, R350A mutant
additional information
inositol 1,4,5-trisphosphate levels in transgenic Arabidopsis thaliana seedlings, roots and hypocotyls, expressing the recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
-
type II enzyme
7 - 7.4
-
assay at
7 - 7.5
-
-
7 - 7.4
-
assay at
7.2
-
assay at
7.4
-
assay at
7.5
-
type I enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
-
-
6.25 - 8.25
additional information
-
pH profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
PIPP enzyme
Manually annotated by BRENDA team
-
PIPP enzyme
Manually annotated by BRENDA team
-
PIPP enzyme
Manually annotated by BRENDA team
-
cortical
Manually annotated by BRENDA team
; low expression of 5PTase13
Manually annotated by BRENDA team
-
PIPP enzyme
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
SDS-PAGE, membrane associated enzyme
45000
-
gel filtration, membrane associated enzyme
47680
calculated from DNA sequence
51000
-
gel filtration in presence of 0.9% cholate, type I enzyme
52000
-
gel filtration in presence of 0.9% cholate, type II enzyme
60000
-
gel filtration and SDS-PAGE, type I enzyme
64900
-
SDS-PAGE
70000
-
SDS-PAGE, gel filtration, membrane associated enzyme
75000
-
gel filtration, SDS-PAGE
81000
-
gel filtration, type II enzyme
90100
-
SDS-PAGE, maltose binding protein MBP-Type I ins(1,4,5)P3 5-phosphatase fusion protein
107000
-
calculated molecular mass, found to be slightly larger in SDS-PAGE
115000
160000
-
gel filtration and SDS-PAGE, type II enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 48000, recombinant His-tagged enzyme, SDS-PAGE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
side-chain modification
additional information
-
protein kinase A and C do not influence activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
in dialysis bags for 20 h
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
labile at 37C, activity is stabilized by phorbol dibutyrate
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, no loss of activity during long term storage
-
-20C, type II stable, type I lost 10% of activity per week
-
-80C, no loss of activity during long term storage
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tag fusion protein expressed in Escherichia coli
membrane associated enzyme
partial purification of membrane bound and soluble enzyme; type I enzyme
-
partial purification of membrane bound enzyme
-
partial purification of type I enzyme
-
purification by a dual tag strategy: cDNA encoding human Type I Ins(1,4,5)P3 5-phosphatase is subcloned into a modified pMAL expression vector. This plasmid produces a recombinant protein in fusion with affinity tags located at its N-terminus, consisting in a maltose binding protein (MPB) and an octa-histidine stretch. The construction is transformed into Escherichia coli BL21 (DE3) expression strain. Yield: 18 mg of pure and stable enzyme starting from a 2 L
-
recombinant enzyme using His-tag
-
recombinant enzymes from Escherichia coli using His-tag
-
recombinant His-tagged catalytic domain from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the tag is cleaved off
-
recombinant His-tagged enzyme from yeast by nickel affinity chromatography; recombinant His-tagged enzyme from yeast by nickel affinity chromatography
recombinant His-tagged full length enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
type I enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
clone BVCT expressed in Escherichia coli
expressed in CHO-K1 cells
-
expressed in COS-7 and CHO cells and Escherichia coli
-
expressed in COS-7 cells
-
expressed in HB 101 host bacteria
-
expressed in Saccharomyces cerevisiae inp51,52,53, lacking inositol 1,4,5-trisphosphate 5-phosphatase activity, rescue of cell viability in cloned cells, His-tag fusion protein expressed in Escherichia coli BL21
-
expressed in Sf9 insect cells
-
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
expression of His-tagged enzyme in Escherichia coli strain JM109
-
expression of His-tagged full length enzyme in Escherichia coli strain BL21(DE3)
-
expression of His-tagged isolated catalytic domain in Escherichia coli strain BL21(DE3)
-
functional expression of the enzyme in transgenic Arabidopsis thaliana plants using the Agrobacterium tumefaciens transfection system
gene 5PTase12, expression of His-tagged full length enzyme in yeast; gene 5PTase13, expression of His-tagged full length enzyme in yeast
His-tag fusion protein expressed in Escherichia coli
His-tagged version expressed in Solanum lycopersicum cv. Micro-Tom
-
overexpressed in host strain, expressed in Drosophila melanogaster S2 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform 5PT12 is preferentially expressed in leaf and mature pollen grains at floral stages 12-14
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C939S
-
eliminates isoprenylation of enzyme which reduces activity towards phosphatidylinositol 4,5-bisphosphate
DELTA407-411
-
predominantly soluble
R343A
-
increased Km and dramatic loss of activity
R350A
-
increased Km
D232A
-
no activity; traces of activity
D384A
-
no activity
E55A
-
no activity
E55Q
-
no activity
F392A
-
50% of activity
H184A
-
traces of activity
H385A
-
no activity
K386A
-
no activity
N18A
-
no activity
P387A
-
traces of activity
T16A
-
100% of activity
V388A
-
traces of activity
DELTA1-119
-
no significant influence on localization of enzyme
DELTA1-311
-
no significant influence on localization of enzyme
DELTA1-433
-
enzyme mainly in cytoplasm
DELTA725-1001
-
enzyme exclusively cytoplasmic
D771A
-
no activity
E631A
-
no activity
H730A
-
no activity
D838G
-
no activity
E597Q
-
site-directed mutagenesis, the mutant enzyme shows an over 140fold increased catalytic efficiency and a 2.4fold reduced affinity for Mg2+ compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
potential target for drugs
molecular biology
At5PTase1 and At5PTase2 genes have nonredundant roles in hydrolyzing inositol second-messenger substrates and regulation of Ins(1,4,5)P3 levels is important during germination and early seedling development; At5PTase1 and At5PTase2 genes have nonredundant roles in hydrolyzing inositol second-messenger substrates and regulation of Ins(1,4,5)P3 levels is important during germination and early seedling development
Show AA Sequence (101 entries)
Please use the Sequence Search for a specific query.