Literature summary for 2.7.7.74 extracted from

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 (2011), J. Bacteriol., 193, 2177-2185.

Cloned(Commentary)

Cloned (Comment)	Organism
cytoplasmic domain of IPCT is expressed in Escherichia coli as a His-tagged fusion protein	Archaeoglobus fulgidus
the cytoplasmic domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34) is produced in Escherichia coli	Archaeoglobus fulgidus

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Archaeoglobus fulgidus
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	Archaeoglobus fulgidus

Crystallization (Comment)

Organism

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

Archaeoglobus fulgidus

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

Archaeoglobus fulgidus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.58	-	CTP	pH and temperature not specified in the publication	Archaeoglobus fulgidus
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)	Archaeoglobus fulgidus
0.87	-	1D-myo-inositol 3-phosphate	pH and temperature not specified in the publication	Archaeoglobus fulgidus
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)	Archaeoglobus fulgidus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	presence of Mg2+ is required for activity, maximal activity is obtained with 20 mM Mg2+	Archaeoglobus fulgidus
Mg2+	required, maximal activity at 20 mM MgCl	Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
CTP + 1L-myo-inositol 1-phosphate	Archaeoglobus fulgidus	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	diphosphate + CDP-1L-myo-inositol	-	?

Organism

Organism	UniProt	Comment	Textmining
Archaeoglobus fulgidus	O29976	-	-

Purification (Commentary)

Purification (Comment)	Organism
the cytoplasmic domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34) is produced in Escherichia coli	Archaeoglobus fulgidus
using metal affinity chromatography and gel filtration	Archaeoglobus fulgidus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
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)	Archaeoglobus fulgidus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
CTP + 1D-myo-inositol 3-phosphate	-	Archaeoglobus fulgidus	diphosphate + CDP-L-myo-inositol	-	?
CTP + 1L-myo-inositol 1-phosphate	-	Archaeoglobus fulgidus	diphosphate + CDP-1L-myo-inositol	-	?
CTP + 1L-myo-inositol 1-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	Archaeoglobus fulgidus	diphosphate + CDP-1L-myo-inositol	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Archaeoglobus fulgidus

Synonyms

Synonyms	Comment	Organism
CTP:inositol-1-phosphate cytidylyltransferase	-	Archaeoglobus fulgidus
IPCT	-	Archaeoglobus fulgidus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
90	95	-	Archaeoglobus fulgidus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
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	Archaeoglobus fulgidus
90	95	maximal activity	Archaeoglobus fulgidus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	7.5	-	Archaeoglobus fulgidus

pH Range

pH Minimum	pH Maximum	Comment	Organism
5.5	8.5	pH 5.5: about 30% of maximal activity, pH 8.5: about 65% of maximal activity	Archaeoglobus fulgidus
6.5	7.5	maximal activity	Archaeoglobus fulgidus

General Information

General Information	Comment	Organism
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	Archaeoglobus fulgidus