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Information on EC 2.7.8.B13 - phosphatidylinositol phosphate synthase
for references in articles please use BRENDA:EC2.7.8.B13
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preliminary BRENDA-supplied EC number
EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.8 Transferases for other substituted phosphate groups
2.7.8.B13 phosphatidylinositol phosphate synthase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 2.7.8.B13
- phospholipid
- tuberculosis
- pernix
-
cdp-dag
- archaea
-
hyperthermophilic
-
aeropyrum
- drug development
- analysis
Reaction Schemes
showSynonyms
phosphatidylinositol phosphate synthase, pgsa1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phosphatidylinositol phosphate synthase
PIP synthase
PIPS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate = CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
CDP-diacylglycerol:1L-myo-inositol 1-phosphate diacylglycerol transferase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CDP-2,3-di-O-phytanyl-sn-glycerol + 1D-myo-inositol 1-phosphate
archaetidylinositol phosphate + CMP
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
additional information
?
-
Substrates: no substrate: 1d-inositol 1-phosphate
Products: -
Products: -
?
CDP-2,3-di-O-phytanyl-sn-glycerol + 1D-myo-inositol 1-phosphate
archaetidylinositol phosphate + CMP
Substrates: -
Products: -
Products: -
?
CDP-2,3-di-O-phytanyl-sn-glycerol + 1D-myo-inositol 1-phosphate
archaetidylinositol phosphate + CMP
-
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: specificity of PIP synthase for lipid substrates
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: specificity of PIP synthase for lipid substrates
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: specificity of PIP synthase for lipid substrates
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: specificity of PIP synthase for lipid substrates
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: specificity of PIP synthase for lipid substrates
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: specificity of PIP synthase for lipid substrates
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: specificity of PIP synthase for lipid substrates
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: specificity of PIP synthase for lipid substrates
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: -
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: specificity of PIP synthase for lipid substrates
Products: -
Products: -
?
CDP-diacylglycerol + 1L-myo-inositol 1-phosphate
CMP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
-
Substrates: specificity of PIP synthase for lipid substrates
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
both Mg2+ and Mn2+ support catalysis. A di-nuclear metal binding site is coordinated by residues D68, D71, D89, and D93 of the conserved sequence motif
Mn2+
both Mg2+ and Mn2+ support catalysis. A di-nuclear metal binding site is coordinated by residues D68, D71, D89, and D93 of the conserved sequence motif
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+-)-1-O-sulfamoyl-myo-inositol
-
16% and 45% inhibition at 1 mM and 5 mM, respectively
1D-myo-inositol 1-monophosphate
-
4% and 45% inhibition at 1 mM and 5 mM, respectively
1L-1-deoxy-1-carboxymethyl-chiro-inositol
-
7% and 41% inhibition at 1 mM and 5 mM, respectively
1L-1-deoxy-1-carboxymethyl-myo-inositol
-
7% and 41% inhibition at 1 mM and 5 mM, respectively
myo-inositol 2-monophosphate
-
10% and 44% inhibition at 1 mM and 5 mM, respectively
(+-)-1-deoxy-1-phosphonomethyl-myo-inositol
-
Ino-C-P, competitive inhibition, 24% and 76% inhibition at 1 mM and 5 mM, respectively
(+-)-1-deoxy-1-phosphonomethyl-myo-inositol
-
leads to growth inhibition
(+-)-1-deoxy-1-[(diethoxyphosphinyl)methyl]-myo-inositol
-
Ino-C-P(OEt)2, 11% and 40% inhibition at 1 mM and 5 mM, respectively
(+-)-1-deoxy-1-[(diethoxyphosphinyl)methyl]-myo-inositol
-
Ino-C-P(OEt)2, leads to growth inhibition
additional information
-
chemical synthesis of four types of inositol 1-phosphate derivatives, all synthesized compounds inhibit PIP synthase activity. The phosphonate analogue of inositol 1-phosphate has the greatest inhibitory effect among the synthesized compounds examined, kinetic analysis. No substrate inhibition by 1L-myo-inositol 1-phosphate
-
additional information
-
no growth inhibition by (+-)-1-O-sulfamoyl-myo-inositol, 1L-1-deoxy-1-carboxymethyl-myo-inositol, and 1 L-1-deoxy-1-carboxymethyl-chiro-inositol
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Structure of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase reveals mechanism of substrate binding and metal catalysis.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
in bacteria, an inositol phospholipid biosynthetic pathway uses precursors inositol 1-phosphate and CDP-DAG to form phosphatidylinositol phosphate (PIP) as intermediate by action of the key enzyme PIP synthase. The intermediate is dephosphorylated to synthesize phosphatidylinositol. The biosynthetic pathway is universal in bacteria which contain inositol phospholipid
metabolism
-
in bacteria, an inositol phospholipid biosynthetic pathway uses precursors inositol 1-phosphate and CDP-DAG to form phosphatidylinositol phosphate (PIP) as intermediate by action of the key enzyme PIP synthase. The intermediate is dephosphorylated to synthesize phosphatidylinositol. The biosynthetic pathway is universal in bacteria which contain inositol phospholipid
metabolism
-
in bacteria, an inositol phospholipid biosynthetic pathway uses precursors inositol 1-phosphate and CDP-DAG to form phosphatidylinositol phosphate (PIP) as intermediate by action of the key enzyme PIP synthase. The intermediate is dephosphorylated to synthesize phosphatidylinositol. The biosynthetic pathway is universal in bacteria which contain inositol phospholipid
metabolism
-
in bacteria, an inositol phospholipid biosynthetic pathway uses precursors inositol 1-phosphate and CDP-DAG to form phosphatidylinositol phosphate (PIP) as intermediate by action of the key enzyme PIP synthase. The intermediate is dephosphorylated to synthesize phosphatidylinositol. The biosynthetic pathway is universal in bacteria which contain inositol phospholipid
metabolism
-
in bacteria, an inositol phospholipid biosynthetic pathway uses precursors inositol 1-phosphate and CDP-DAG to form phosphatidylinositol phosphate (PIP) as intermediate by action of the key enzyme PIP synthase. The intermediate is dephosphorylated to synthesize phosphatidylinositol. The biosynthetic pathway is universal in bacteria which contain inositol phospholipid
metabolism
-
distinct pathway for the biosynthesis of phosphatidylinositol in mycobacteria via phosphatidylinositol phosphate (PIP) and phosphatidylinositol phosphate synthase activity
metabolism
-
distinct pathway for the biosynthesis of phosphatidylinositol in mycobacteria via phosphatidylinositol phosphate (PIP) and phosphatidylinositol phosphate synthase activity
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PIPS_MYCBP
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
217
0
23252
Swiss-Prot
-
PIPS_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
217
0
23252
Swiss-Prot
other Location (Reliability: 4)
AIPS_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
195
4
22095
Swiss-Prot
other Location (Reliability: 5)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of PgsA1 in absence of substrates (2.9 A), in complex with Mn2+ and citrate (1.9 A), and with the CDP-DAG substrate (1.8 A). The nucleotide moiety of the substrate is bound into a cleft formed by transmembrane helices 1-3, lined by G72, A75, and G85 and exposed to solvent. The long acyl chains of the substrate are disordered
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
an artificial gene construct for a protein homologous to phosphatidylinositol phosphate synthase of Mycobacterium tuberculosis and archaetidylinositol phosphate synthase of Methanothermobacter thermautotrophicus is cloned in Escherichia coli and introduced into Corynebacterium glutamicum cells. The recombinant cells show afterwards both, phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase activities, 175 pmol/h/mg and 174 pmol/h/mg, respectively, but no phosphatidylinositol synthase activity is detected, overview
additional information
-
an artificial gene construct for a protein homologous to phosphatidylinositol phosphate synthase of Mycobacterium tuberculosis and archaetidylinositol phosphate synthase of Methanothermobacter thermautotrophicus is cloned in Escherichia coli and introduced into Propionibacterium acnes cells. The recombinant cells show afterwards both, phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase activities, 88 pmol/h/mg and 14 pmol/h/mg, respectively, but no phosphatidylinositol synthase activity is detected, overview
additional information
-
an artificial gene construct for a protein homologous to phosphatidylinositol phosphate synthase of Mycobacterium tuberculosis and archaetidylinositol phosphate synthase of Methanothermobacter thermautotrophicus is cloned in Escherichia coli and introduced into Mycobacterium bovis cells. The recombinant cells show afterwards both, phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase activities, 138 pmol/h/mg and 5 pmol/h/mg, respectively, but no phosphatidylinositol synthase activity is detected, overview
additional information
-
an artificial gene construct for a protein homologous to phosphatidylinositol phosphate synthase of Mycobacterium tuberculosis and archaetidylinositol phosphate synthase of Methanothermobacter thermautotrophicus is cloned in Escherichia coli and introduced into Rhodococcus equi cells. The recombinant cells show afterwards both, phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase activities, 124 pmol/h/mg and 33 pmol/h/mg, respectively, but no phosphatidylinositol synthase activity is detected, overview
additional information
-
an artificial gene construct for a protein homologous to phosphatidylinositol phosphate synthase of Mycobacterium tuberculosis and archaetidylinositol phosphate synthase of Methanothermobacter thermautotrophicus is cloned in Escherichia coli and introduced into Streptomyces avermitilis cells. The recombinant cells show afterwards both, phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase activities, 76 pmol/h/mg and 20 pmol/h/mg, respectively, but no phosphatidylinositol synthase activity is detected, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
synthesis of substrate 1l-myo-inositol 1-phosphate using a solution containing recombinant 1l-myo-inositol 1-phosphate synthase derived from the hyperthermophilic archaeon Aeropyrum pernix
drug development
-
the enzyme is a promising target for the development of anti-mycobacterium drugs
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morii, H.; Ogawa, M.; Fukuda, K.; Taniguchi, H.
Ubiquitous distribution of phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase in bacteria and archaea, which contain inositol phospholipid
Biochem. Biophys. Res. Commun.
443
86-90
2013
Corynebacterium glutamicum, Cutibacterium acnes, Homo sapiens, Mycobacterium tuberculosis variant bovis, Prescottella equi, Saccharolobus solfataricus (Q7LXU6), Saccharomyces cerevisiae, Streptomyces avermitilis
brenda
Morii, H.; Okauchi, T.; Nomiya, H.; Ogawa, M.; Fukuda, K.; Taniguchi, H.
Studies of inositol 1-phosphate analogues as inhibitors of the phosphatidylinositol phosphate synthase in mycobacteria
J. Biochem.
153
257-266
2013
Mycobacterium tuberculosis, Mycolicibacterium smegmatis
-
brenda
Grave, K.; Bennett, M.D.; Hoegbom, M.
Structure of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase reveals mechanism of substrate binding and metal catalysis
Commun. Biol.
2
175
2019
Mycobacterium tuberculosis (P9WPG7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPG7)
brenda
Morii, H.; Nishimura, T.; Takeo, M.; Katayama, C.; Nakai, K.
Preparation of 1l-myo-inositol 1-phosphate as a substrate of phosphatidylinositol phosphate synthase
J. Uoeh
40
217-224
2018
Mycobacterium tuberculosis variant bovis (A0A0H3MFZ3)
brenda
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