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
-
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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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
substituted phospho group transfer
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-
-
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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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Glycerophospholipid metabolism
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Inositol phosphate metabolism
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lipid metabolism
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Metabolic pathways
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phosphatidylinositol biosynthesis II (eukaryotes)
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superpathway of phospholipid biosynthesis II (plants)
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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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-
-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
guinea pig
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
chicken
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-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
turkey
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
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
castor bean
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
; strain V2S
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-
Manually annotated by BRENDA team
strain V2S
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-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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
-
-
-
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
-
6% of the activity with CDP-1-stearoyl-2-oleoylglycerol
-
-
r
CDP-1-stearoyl-2-arachidonoylglycerol + myo-inositol
CMP + 1-stearoyl-2-arachidonoylphosphatidylinositol
show the reaction diagram
-
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
-
-
-
-
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
-
conversion of 25.1% CDP-diacylglycerol (non-significant), microsomal fraction, 30C, 20 min
-
-
?
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
-
-
?
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
-
67% of the activity on myo-inositol
-
-
?
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
-
9% of the activity with CDP-1-stearoyl-2-oleoylglycerol
-
-
r
CDP-didecanoyl-sn-glycerol + myo-inositol
CMP + didecanoylphosphatidylinositol
show the reaction diagram
-
preferred substrate
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-
r
CDP-diheptadecanoylglycerol + D-myo-inositol
CMP + 1,2-diheptadecanoyl-phosphatidyl-1D-myo-inositol
show the reaction diagram
-
-
-
?
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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-
-
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r
CDP-dipalmitoylglycerol + D-myo-inositol
CMP + 1,2-dipalmitoyl-phosphatidyl-1D-myo-inositol
show the reaction diagram
-
-
-
?
CDP-distearoylglycerol + myo-inositol
CMP + distearoylphosphatidylinositol
show the reaction diagram
-
38% of the activity with CDP-1-stearoyl-2-oleoylglycerol
-
-
r
CDPdipalmitoyl-sn-glycerol + myo-inositol
CMP + dipalmitoylphosphatidylinositol
show the reaction diagram
-
70% of the activity with CDP-1-stearoyl-2-oleoylglycerol
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-
r
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
CDP-diacylglycerol + D-myo-inositol
CMP + phosphatidyl-1D-myo-inositol
show the reaction diagram
Q8GUK6, Q8LBA6
key step in lipid biosynthesis
-
-
?
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
-
Hecameg, above 5 mM
AMP
-
non-competitive inhibition
bovine serum albumin
-
slight inhibition
-
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
additional information
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
-
pH 8.3, 37C
0.029 - 0.045
2-deoxy-CDP-diacylglycerol
0.03
CDP-1-stearoyl-2-oleoylglycerol
-
pH 8.3, 37C
0.0095 - 0.21
CDP-diacylglycerol
0.06
CDP-didecanoyl-sn-glycerol
-
-
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
-
pH 8.6, 37C
-
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
-
pH 8.3, 37C
1.4
ATP
-
pH 9.0, 37C
0.6
CaCl2
-
pH 9.0, 37C
4
CDP
-
pH 9.0, 37C
1.8
CTP
-
pH 9.0, 37C
0.2
diphosphate
1.6
GTP
-
pH 9.0, 37C
0.6 - 0.8
phosphate
1.4
TTP
-
pH 9.0, 37C
3.8
UDP
-
pH 9.0, 37C
1.4
UTP
-
pH 9.0, 37C
2
ZnCl2
-
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
-
-
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
-
optimum for exchange reaction
7.7
-
CTP and phosphatidic acid as substrate
8
-
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
-
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
-
exchange reaction exhibits reduced activity above
50
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89% of maximum activity, pH 7.8, 10 min preincubation
60
-
82% of maximum activity, pH 7.8, 10 min preincubation
70
-
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
-
-
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
little or no activity in the plastids
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23740
theoretical
24820
-
calculated molecular mass from the cloned PI synthase gene
27800
calculated from cDNA
60000
-
SDS-PAGE
150000 - 200000
-
gel filtration
300000
-
partially purified enzyme, ultrafiltration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 50
-
thermal denaturation at higher temperatures, half-life at 50C 30 min
50
-
half-life without substrates 20 min
70
-
10 min, 80% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is stable for at least 4 cycles of freezing and thawing
-
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
-
stable to at least 2 cycles of freezing and thawing with no loss in enzyme activity
-
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
-
-20C, substrate and dithioerythritol protects the enzyme activity for several days
-
-60C, frozen and stored or frozen in liquid nitrogen and subsequently stored, over 50% activity is lost after 24 h
-
-70C, substantial loss of enzymic activity when stored for more than 48 h
-
-80C, can be stored for a few days without appreciable loss of activity, inactivated gradually during storage for longer periods
-
-80C, frozen in liquid N2 and stored, no loss of activity is detected during storage for up to 2 months
-
-80C, glycerol stabilizes PI synthase to storage, stable to storage for at least 3 months
-
-80C, no appreciable loss of PI synthase activity detected for up to at least 6 months
-
-80C, partially purified enzyme can be stored for at least 3 months without loss of activity
-
-80C, purified enzyme is completely stable for at least 6 months
-
-80C, regularly frozen in liqid N2, no detectable loss of activity is experienced during storage at -80C for up to 2 months
-
4C, 67% of the activity remains after 3 days
-
4C, stored on ice, 10% of the activity is lost during 24 h
-
8C, enzyme is 100% stabe for at least 3 days of storage
-
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
-
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
-
; 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
-
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
-
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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