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 taxonomic range for the selected organisms is: Archaeoglobus fulgidus The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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.
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
the enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
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
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
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
the enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments
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
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
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
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
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
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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
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
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
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