Information on EC 2.7.8.11 - CDP-diacylglycerol-inositol 3-phosphatidyltransferase

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

EC NUMBER
COMMENTARY hide
2.7.8.11
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RECOMMENDED NAME
GeneOntology No.
CDP-diacylglycerol-inositol 3-phosphatidyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CDP-diacylglycerol + myo-inositol = CMP + 1-phosphatidyl-1D-myo-inositol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
substituted phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-phosphoinositide biosynthesis
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D-myo-inositol (1,4,5)-trisphosphate biosynthesis
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phosphatidylinositol biosynthesis II (eukaryotes)
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superpathway of phospholipid biosynthesis II (plants)
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lipid metabolism
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Inositol phosphate metabolism
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Glycerophospholipid metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
CDP-diacylglycerol:myo-inositol 3-phosphatidyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9027-01-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
animal
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
chicken
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
no activity in Escherichia coli
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Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
yeast, PI synthase mutant strain D501-1
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
snake
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain V2S
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-stearoyl-2-arachidonoylphosphatidylinositol + CMP
CDP-1-stearoyl-2-arachidonoylglycerol + myo-inositol
show the reaction diagram
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r
2-deoxy-CDP-diacylglycerol + myo-inositol
CMP + ?
show the reaction diagram
CDP-1-arachidonoyl-2-stearoylglycerol + myo-inositol
CMP + 1-arachidonoyl-2-stearoylphosphtidylinositol
show the reaction diagram
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6% of the activity with CDP-1-stearoyl-2-oleoylglycerol
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r
CDP-1-stearoyl-2-arachidonoylglycerol + myo-inositol
CMP + 1-stearoyl-2-arachidonoylphosphatidylinositol
show the reaction diagram
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4% of the activity with CDP-1-stearoyl-2-oleoylglycerol
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r
CDP-1-stearoyl-2-oleoylglycerol + myo-inositol
CMP + 1-stearoyl-2-oleoylphosphatidylinositol
show the reaction diagram
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r
CDP-diacylglycerol + 1D-chiro-inositol
CMP + phosphatidyl-1D-chiro-inositol
show the reaction diagram
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conversion of 30.9% CDP-diacylglycerol (utilization significant compared to background, p: 0.05), microsomal fraction, 30C, 20 min
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?
CDP-diacylglycerol + 1L-chiro-inositol
CMP + phosphatidyl-1L-chiro-inositol
show the reaction diagram
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conversion of 25.1% CDP-diacylglycerol (non-significant), microsomal fraction, 30C, 20 min
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?
CDP-diacylglycerol + allo-inositol
CMP + phosphatidyl-allo-inositol
show the reaction diagram
CDP-diacylglycerol + D-chiro-inositol
CMP + phosphatidyl-chiro-inositol
show the reaction diagram
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82% of the activity on myo-inositol
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?
CDP-diacylglycerol + D-myo-inositol
CMP + phosphatidyl-1D-myo-inositol
show the reaction diagram
CDP-diacylglycerol + epi-inositol
CMP + phosphatidyl-epi-inositol
show the reaction diagram
CDP-diacylglycerol + L-chiro-inositol
CMP + phosphatidyl-chiro-inositol
show the reaction diagram
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67% of the activity on myo-inositol
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?
CDP-diacylglycerol + muco-inositol
CMP + phosphatidyl-muco-inositol
show the reaction diagram
CDP-diacylglycerol + myo-inositol
CMP + phosphatidyl-1D-myo-inositol
show the reaction diagram
CDP-diacylglycerol + myo-inositol
CMP + phosphatidyl-myo-inositol
show the reaction diagram
CDP-diacylglycerol + scyllo-inositol
CMP + phosphatidyl-scyllo-inositol
show the reaction diagram
CDP-diarachidonoylglycerol + myo-inositol
CMP + diarachidonoylphosphatidylinositol
show the reaction diagram
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9% of the activity with CDP-1-stearoyl-2-oleoylglycerol
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r
CDP-didecanoyl-sn-glycerol + myo-inositol
CMP + didecanoylphosphatidylinositol
show the reaction diagram
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preferred substrate
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r
CDP-diheptadecanoylglycerol + D-myo-inositol
CMP + 1,2-diheptadecanoyl-phosphatidyl-1D-myo-inositol
show the reaction diagram
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?
CDP-dilinoleoylglycerol + D-myo-inositol
CMP + 1,2-dilinoleoyl-phosphatidyl-1D-myo-inositol
show the reaction diagram
CDP-dioleoylglycerol + D-myo-inositol
CMP + 1,2-dioleoyl-phosphatidyl-1D-myo-inositol
show the reaction diagram
CDP-dioleoylglycerol + myo-inositol
CMP + dioleoylphosphatidylinositol
show the reaction diagram
CDP-dipalmitoyl-sn-glycerol + myo-inositol
CMP + dipalmitoylphosphatidylinositol
show the reaction diagram
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r
CDP-dipalmitoylglycerol + D-myo-inositol
CMP + 1,2-dipalmitoyl-phosphatidyl-1D-myo-inositol
show the reaction diagram
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?
CDP-distearoylglycerol + myo-inositol
CMP + distearoylphosphatidylinositol
show the reaction diagram
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38% of the activity with CDP-1-stearoyl-2-oleoylglycerol
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r
CDPdipalmitoyl-sn-glycerol + myo-inositol
CMP + dipalmitoylphosphatidylinositol
show the reaction diagram
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70% of the activity with CDP-1-stearoyl-2-oleoylglycerol
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r
additional information
?
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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
CDP-diacylglycerol + D-myo-inositol
CMP + phosphatidyl-1D-myo-inositol
show the reaction diagram
Q8GUK6, Q8LBA6
key step in lipid biosynthesis
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?
CDP-diacylglycerol + myo-inositol
CMP + phosphatidyl-1D-myo-inositol
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-O-(N-heptyl-carbamoyl)methyl-alpha-D-glucopyranoside
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Hecameg, above 5 mM
AMP
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non-competitive inhibition
bovine serum albumin
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slight inhibition
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CaCl2
CDP-diacylglycerol
CDP-dipalmitoylglyceride
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above 1.2 mM
Cetylpyridinium chloride
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Cetyltrimethylammonium bromide
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strong inhibition
diphosphate
hexachlorocyclohexane
Inosose-2
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competitive to inositol
Inostamycin
iodoacetamide
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iodoacetate
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myo-inositol
N-ethylmaleimide
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p-chloromercuribenzene sulfonate
phosphate
Sodium dodecyl sulfate
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Triton X-100
ZnCl2
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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enhances enzyme activity
Triton X-100
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
1-stearoyl-2-arachidonoylglycerol
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pH 8.3, 37C
0.029 - 0.045
2-deoxy-CDP-diacylglycerol
0.03
CDP-1-stearoyl-2-oleoylglycerol
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pH 8.3, 37C
0.0095 - 0.21
CDP-diacylglycerol
0.06
CDP-didecanoyl-sn-glycerol
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0.01929 - 0.0195
CDP-dipalmitin
1.35
CDP-dipalmitoylglyceride
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pH 8.5, 37C
0.16
CDP-distearoylglycerol
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pH 8.3, 37C
0.17
CDPdiglyceride
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pH 8.6, 37C
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0.022 - 2.8
CMP
0.05
dipalmitoyl-sn-glycerol
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pH 8.3, 37C
0.015 - 2.5
myo-inositol
0.71
myo-inositol CDP
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.1
ADP
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pH 9.0, 37C
0.04
AMP
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pH 8.3, 37C
1.4
ATP
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pH 9.0, 37C
0.6
CaCl2
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pH 9.0, 37C
4
CDP
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pH 9.0, 37C
1.8
CTP
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pH 9.0, 37C
0.2
diphosphate
1.6
GTP
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pH 9.0, 37C
0.6 - 0.8
phosphate
1.4
TTP
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pH 9.0, 37C
3.8
UDP
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pH 9.0, 37C
1.4
UTP
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pH 9.0, 37C
2
ZnCl2
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pH 9.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000023
wild-type, in vitro phosphatidylinositol synthesis, yeast membrane extracts after overexpression
0.000036
hybrid Hy4, in vitro phosphatidylinositol synthesis, yeast membrane extracts after overexpression
0.0008 - 0.0009
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0.001 - 0.002
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0.002 - 0.009
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additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
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pH optimum for reverse reaction
6.5 - 7
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pH optimum in reverse direction
7
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optimum for exchange reaction
7.7
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CTP and phosphatidic acid as substrate
8
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highest activity in Tris buffer, only 43% of the activity in glycine/NaOH buffer at pH 9.5
8.5 - 9
9
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in glycylglycine/NaOH or glycine/NaOH buffer
9.5
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glycine NaOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10.5
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6.5 - 10
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little or no activity detectable at pH 6.3 and pH 5.5
6.5 - 9.5
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at pH 7.0 activity is approximately one-fourth that observed at optimum pH 8.8, enzyme is equally active at pH 8.5
7.3 - 8.4
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30C, 90% of maximum activity; about 90% of maximum activity within this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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exchange reaction exhibits reduced activity above
50
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89% of maximum activity, pH 7.8, 10 min preincubation
60
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82% of maximum activity, pH 7.8, 10 min preincubation
70
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79% of maximum activity, pH 7.8, 10 min preincubation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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carcinoma cell
Manually annotated by BRENDA team
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NIH3T3 cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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little or no activity in the plastids
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24820
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calculated molecular mass from the cloned PI synthase gene
27800
calculated from cDNA
60000
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SDS-PAGE
150000 - 200000
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gel filtration
300000
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partially purified enzyme, ultrafiltration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bound to the cofactor NAD+, space group P42(1)2, cell dimensions a = 116.2, b = 116.2, c = 64.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 50
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thermal denaturation at higher temperatures, half-life at 50C 30 min
50
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half-life without substrates 20 min
70
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10 min, 80% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is stable for at least 4 cycles of freezing and thawing
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addition of bovine serum albumin is necessary in assaying the enzyme
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inactivation caused by repeated freezing and thawing or by contact with detergent is prevented by addition of dithiothreitol and CDPdiacyl-sn-glycerol
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loses activity when the lipids are removed
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stable to at least 2 cycles of freezing and thawing with no loss in enzyme activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, frozen and stored or frozen in liquid nitrogen and subsequently stored, over 50% activity is lost after 24 h
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-20C, substrate and dithioerythritol protects the enzyme activity for several days
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-60C, frozen and stored or frozen in liquid nitrogen and subsequently stored, over 50% activity is lost after 24 h
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-70C, substantial loss of enzymic activity when stored for more than 48 h
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-80C, can be stored for a few days without appreciable loss of activity, inactivated gradually during storage for longer periods
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-80C, frozen in liquid N2 and stored, no loss of activity is detected during storage for up to 2 months
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-80C, glycerol stabilizes PI synthase to storage, stable to storage for at least 3 months
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-80C, no appreciable loss of PI synthase activity detected for up to at least 6 months
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-80C, partially purified enzyme can be stored for at least 3 months without loss of activity
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-80C, purified enzyme is completely stable for at least 6 months
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-80C, regularly frozen in liqid N2, no detectable loss of activity is experienced during storage at -80C for up to 2 months
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4C, 67% of the activity remains after 3 days
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4C, stored on ice, 10% of the activity is lost during 24 h
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8C, enzyme is 100% stabe for at least 3 days of storage
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
as bacterial membrane pellets, no further specific purification possible; as bacterial membrane pellets, no further specific purification possible
partially
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; AtPIS1 cDNA cloned in Escherichia coli XL-1 Blue, functional complementation of Saccharomyces cerevisiae wild-type strain D501-1
; AtPIS1 cloned and expressed in Escherichia coli, a host naturally devoid of phosphatidylinositol; cloned and expressed in Escherichia coli
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; cDNA cloned by functional complementation in Saccharomyces cerevisiae
; gene AtPIS1 cDNA cloned and expressed in Escherichia coli
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; highly spliced gene with 9 exons, cDNA encodes 207 amino acids, from mRNA in pCRII-Blunt-TOPO for cloning and sequencing (transformation of Escherichia coli TOP10 and DH5alpha)
; highly spliced gene with 9 exons, cDNA encodes 209 amino acids, from total RNA in pCR-BluntII-Topo for cloning and sequencing (transformation of Escherichia coli TOP10 and DH5alpha), in p413 for complementation studies in Saccharomyces cerevisiae
cDNA cloned by functional complementation of a Saccharomyces cerevisiae mutant
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disruption of the PIS locus in the genome is lethal
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expressed in Escherichia coli
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from flower and silique cDNA, in pGEM-T-Easy for sequencing, in pET28b for inducible expression in Escherichia coli C43(DE3), in pUC18-ENTR-EYFP for introduction of C-terminal EYFP-tag followed by subcloning into pCAMBIA3300-0GC for Agrobacterium tumefaciens-mediated transformation of Arabidopsis thaliania plants or transient expression in onion (Allium cepa) epidermal sections; from flower and silique cDNA, in pGEM-T-Easy for sequencing, in pET28b for inducible expression in Escherichia coli C43(DE3), in pUC18-ENTR-EYFP or -CFP for introduction of C-terminal EYFP- or CFP-tag followed by subcloning into pCAMBIA3300-0GC for Agrobacterium tumefaciens-mediated transformation of Arabidopsis thaliania plants or transient expression in onion (Allium cepa) epidermal sections
gene PIS cloned with pUC8 and expressed in Escherichia coli HB101
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rat PIS expressed in mouse NIH3T3 fibroblasts by transfection with a FLAG-tagged PIS cDNA using the vector pcDNA3
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tbINO, the coding sequence of ino1 amplified by PCR, cloned into expression vector pET-15b and overproduced in Escherichia coli BL21 (DE3)
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yeast cDNA S45885 used to search, pis1 cDNA cloned and expressed in COS-7 cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C148W
polymorphism of unclear relevance, amplified from plant cDNA, mismatch with annotated genomic sequence
S111C
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missense mutation leads to lens opaque (lop) phenotype. Mutation is located in the catalytic domain of the 213 amino acid phosphatidylinositol (PI) synthase enzyme
Hy3
hybrid construct of 57 N-terminal amino acids from Saccharomyces cerevisiae PIS and 159 C-terminal amino acids from PfPIS, no in vitro activity, 60% complementation of in vivo activity in yeast lacking endogenous PIS gene compared to ScPIS complementation efficiency (100%)
Hy4
hybrid construct of 14 N-terminal amino acids from Saccharomyces cerevisiae PIS and 202 C-terminal amino acids from PfPIS, 37% complementation of in vivo activity in yeast lacking endogenous PIS gene compared to ScPIS complementation efficiency (100%)
H114Q
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oligonucleotide-mediated site-directed mutagenesis, substitution of amino acid at position 114 from His (CAC) + Gln (CAA) results in a 200fold increase in Km of the enzyme for myo-inositol, making cells auxotrophic for myo-inositol
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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