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Information on EC 2.7.7.74 - 1L-myo-inositol 1-phosphate cytidylyltransferase
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2.7.7.74 1L-myo-inositol 1-phosphate cytidylyltransferaseIUBMB Comments
In many organisms this activity is catalysed by a bifunctional enzyme. The cytidylyltransferase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
ctp:inositol-1-phosphate cytidylyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CDP-inositol:inositol-1-phosphate transferase
bifunctional enzyme CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase
CTP:inositol-1-phosphate cytidylyltransferase
IPCT
Tmari_1425
CTP:inositol-1-phosphate cytidylyltransferase
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)
CTP:inositol-1-phosphate cytidylyltransferase
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)
CTP:inositol-1-phosphate cytidylyltransferase
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)
CTP:inositol-1-phosphate cytidylyltransferase
no CDP-inositol:inositol-1-phosphate transferase activity detected
CTP:inositol-1-phosphate cytidylyltransferase
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)
IPCT
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)
IPCT
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)
IPCT
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)
IPCT
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + 1L-myo-inositol 1-phosphate = diphosphate + CDP-1L-myo-inositol
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
CTP:1L-myo-inositol 1-phosphate cytidylyltransferase
In many organisms this activity is catalysed by a bifunctional enzyme. The cytidylyltransferase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments.
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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
CDP-glycerol + 1L-myo-inositol 1-phosphate
CMP + 1-(1X-glyceryl) myo-inosityl phosphate 3-phosphate
-
-
-
?
additional information
?
-
-
enzyme is highly specific for CTP and inositol-1-phosphate. No substrates: ATP, GTP, UTP, myo-inositol, glycerol, DL-glycerol-phosphate, alpha-glucose-1-phosphate, beta-glucose-1-phosphate, glucose-6-phosphate, fructose-6-phosphate, fructose-1-phosphate and galactose-1-phosphate
-
-
?
CTP + 1D-myo-inositol 3-phosphate
diphosphate + CDP-L-myo-inositol
-
-
-
?
CTP + 1D-myo-inositol 3-phosphate
diphosphate + CDP-L-myo-inositol
the enzyme is involved in the synthesis of di-myo-inositol phosphate. Archaeoglobus fulgidus accumulates di-myo-inositol phosphate and diglycerol phosphate in response to heat and osmotic stresses, respectively, and the level of glycero-phospho-myo-inositol increases primarily when the two stresses are combined
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase. The cytidylyltransferase is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The di-myo-inositol-1,3'-phosphate-1'-phosphate synthase domain uses only 1L-myo-inositol 1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myo-inositol, are recognized as alcohol donors
structural characterization of products by nuclear magnetic resonance
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
-
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
-
-
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase. The cytidylyltransferase is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The di-myo-inositol-1,3'-phosphate-1'-phosphate synthase domain uses only 1L-myo-inositol 1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myo-inositol, are recognized as alcohol donors
structural characterization of products by nuclear magnetic resonance
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of the solute bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase. The cytidylyltransferase is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The di-myo-inositol-1,3'-phosphate-1'-phosphate synthase domain uses only 1L-myo-inositol 1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myo-inositol, are recognized as alcohol donors
structural characterization of products by nuclear magnetic resonance
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of di-myo-inositol 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
no CDP-inositol:inositol-1-phosphate transferase activity detected. myo-Inositol is not a substrate
structural characterization of products by nuclear magnetic resonance
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase. The cytidylyltransferase is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The di-myo-inositol-1,3'-phosphate-1'-phosphate synthase domain uses only 1L-myo-inositol 1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myo-inositol, are recognized as alcohol donors
structural characterization of products by nuclear magnetic resonance
-
?
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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
CTP + 1D-myo-inositol 3-phosphate
diphosphate + CDP-L-myo-inositol
the enzyme is involved in the synthesis of di-myo-inositol phosphate. Archaeoglobus fulgidus accumulates di-myo-inositol phosphate and diglycerol phosphate in response to heat and osmotic stresses, respectively, and the level of glycero-phospho-myo-inositol increases primarily when the two stresses are combined
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of the solute bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of di-myo-inositol 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
CTP + 1L-myo-inositol 1-phosphate
diphosphate + CDP-1L-myo-inositol
the enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
presence of Mg2+ is required for activity, maximal activity is obtained with 20 mM Mg2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate
-
i.e. CHAPS, or Triton X-100, absolutely required
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.87
1D-myo-inositol 3-phosphate
pH and temperature not specified in the publication
0.87
1L-myo-inositol 1-phosphate
90°C, pH 7.0, cytoplasmic CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34)
0.58
CTP
90°C, pH 7.0, cytoplasmic CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62.9
90°C, pH 7.0, cytoplasmic CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
pH 5.5: about 30% of maximal activity, pH 8.5: about 65% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 100
activity of the enzyme is undetectable at temperatures below 60°C, and maximal activity is reached between 90 and 95°C, at 100°C about 25% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional enzyme CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (EC 2.7.7.74/EC 2.7.8.34)
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
protein may transiently associate with its membrane-embedded partner phospho-DIP synthase
-
brenda
-
protein may transiently associate with its membrane-embedded partner phospho-DIP synthase
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
deleting the gene encoding the key enzyme in di-myo-inositol phosphate synthesis, CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, abolishes di-myo-inositol phosphate synthesis. Mutants deficient in di-myo-inositol phosphate use aspartate to cope with heat stress
physiological function
physiological function
di-myo-inositol phosphate is part of the strategy used by Thermococcus kodakarensis to cope with heat stress, and aspartate can be used as an alternative solute of similar efficacy
physiological function
the enzyme is involved in synthesis of di-myo-inositol phosphate. Archaeoglobus fulgidus accumulates di-myo-inositol phosphate and diglycerol phosphate in response to heat and osmotic stresses, respectively, and the level of glycero-phospho-myo-inositol increases primarily when the two stresses are combined
physiological function
the bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (EC 2.7.7.74/EC 2.7.8.34) is involved in biosynthesis of bis(1L-myo-inositol) 1,3-phosphate
physiological function
the enzyme is involved in biosynthesis of the solute bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
Show AA Sequence and Transmembrane Helices (861 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme in the apo form is solved to a 1.9 A resolution. The structure of IPCT is composed of a central seven-stranded mixed beta-sheet, of which six beta-strands are parallel, surrounded by six alpha-helices, a fold reminiscent of the dinucleotide-binding Rossmann fold
crystallization of the CTP:inositol-1-phosphate cytidylyltransferase domain in the apo form. The crystals diffracted to 2.4 A resolution using a synchrotron source and belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 154.7, b = 83.9, c = 127.7 A
hanging-drop vapor diffusion method at 20°C, X-ray structure of the cytoplasmic CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34). The structure of the enzyme in the apo form was solved to a 1.9 A resolution. The structure of CTP:inositol-1-phosphate cytidylyltransferase is composed of a central seven-stranded mixed beta-sheet, of which six beta-strands are parallel, surrounded by six alpha-helices, a fold reminiscent of the dinucleotide-binding Rossmann fold
structure shows a conserved motif of sugar nucleotide transferases (COG1213) with a structurally reinforced C-terminal Cys bonded to the core of the protein. During catalysis, the conserved Asp107 serves as an electrostatic anchor to which the metal ion (most likely Mg2+) binds. Upon binding, the triphosphate group of the nucleotide interacts with a metal ion as well as the phosphate of the inositol. The O atom of the inositol phosphate group that is polarized by this interaction attacks the triphosphate and causes its cleavage to release the diphosphate group. Lys24 stabilizes the developing negative charge in the transition state and Arg14 serves as a release agent
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification CTP:inositol-1-phosphate cytidylyltransferase domain
the cytoplasmic domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34) is produced in Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytoplasmic domain of IPCT is expressed in Escherichia coli as a His-tagged fusion protein
the CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (EC 2.7.7.74/EC 2.7.8.34) is cloned and expressed in Escherichia coli
the cytoplasmic domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34) is produced in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Borges, N.; Goncalves, L.G.; Rodrigues, M.V.; Siopa, F.; Ventura, R.; Maycock, C.; Lamosa, P.; Santos, H.
Biosynthetic pathways of inositol and glycerol phosphodiesters used by the hyperthermophile Archaeoglobus fulgidus in stress adaptation
J. Bacteriol.
188
8128-8135
2006
Archaeoglobus fulgidus (O29976)
brenda
Rodrigues, M.V.; Borges, N.; Henriques, M.; Lamosa, P.; Ventura, R.; Fernandes, C.; Empadinhas, N.; Maycock, C.; da Costa, M.S.; Santos, H.
Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles
J. Bacteriol.
189
5405-5412
2007
Archaeoglobus fulgidus (O29976), Aquifex aeolicus (O67379), Rubrobacter xylanophilus (Q1AWQ0), Thermococcus kodakarensis (Q5JDA9), Pyrococcus furiosus (Q8U1Z6)
brenda
Borges, N.; Matsumi, R.; Imanaka, T.; Atomi, H.; Santos, H.
Thermococcus kodakarensis mutants deficient in di-myo-inositol phosphate use aspartate to cope with heat stress
J. Bacteriol.
192
191-197
2010
Thermococcus kodakarensis (Q5JDA9)
brenda
Brito, J.A.; Borges, N.; Santos, H.; Archer, M.
Production, crystallization and preliminary X-ray analysis of CTP:inositol-1-phosphate cytidylyltransferase from Archaeoglobus fulgidus
Acta Crystallogr. Sect. F
66
1463-1465
2010
Archaeoglobus fulgidus (O29976), Archaeoglobus fulgidus
brenda
Brito, J.A.; Borges, N.; Vonrhein, C.; Santos, H.; Archer, M.
Crystal structure of Archaeoglobus fulgidus CTP:inositol-1-phosphate cytidylyltransferase, a key enzyme for di-myo-inositol-phosphate synthesis in (hyper)thermophiles
J. Bacteriol.
193
2177-2185
2011
Archaeoglobus fulgidus (O29976), Archaeoglobus fulgidus
brenda
Kurnasov, O.; Luk, H.; Roberts, M.; Stec, B.
Structure of the inositol-1-phosphate cytidylyltransferase from Thermotoga maritima
Acta Crystallogr. Sect. D
69
1808-1817
2013
Thermotoga maritima (G4FFF4), Thermotoga maritima DSM 3109 (G4FFF4)
brenda
Jorge, C.; Borges, N.; Santos, H.
A novel pathway for the synthesis of inositol phospholipids uses cytidine diphosphate (CDP)-inositol as donor of the polar head group
Environ. Microbiol.
17
2492-2504
2015
Rhodothermus marinus
-
brenda
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