Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

5.5.1.4: inositol-3-phosphate synthase

This is an abbreviated version!
For detailed information about inositol-3-phosphate synthase, go to the full flat file.

Word Map on EC 5.5.1.4

Reaction

D-glucose 6-phosphate
=
1D-myo-inositol 3-phosphate

Synonyms

1D-myo-inositol 3-phosphate synthase, 1L-myo-Inositol-1-phosphate synthase, AtMIPS1, AtMIPS2-1, AtMIPS3, CaMIPS1, CaMIPS2, D-Glucose 6-phosphate cycloaldolase, D-Glucose 6-phosphate-1L-myoinositol 1-phosphate cyclase, D-Glucose 6-phosphate-1L-myoinositol 1-phosphate cycloaldolase, D-Glucose 6-phosphate-L-myo-inositol 1-phosphate cyclase, D-Glucose-6-phosphate,L-myo-inositol-1-phosphate cycloaldolase, D-myo-inositol-3-phosphate synthase, Glucocycloaldolase, Glucose 6-phosphate cyclase, Glucose-6-phosphate inositol monophosphate cycloaldolase, INO-1, INO-2, INO1, Ino1p, iNOS, Inositol 1-phosphate synthase, Inositol 1-phosphate synthetase, inositol 3-phosphate synthase, inositol phosphate synthase, inositol-1-phosphate synthase, inositol-3-phosphate synthase, INPS, INPS1, INS (3) P1 synthase, IP synthase, IPS, L-myo-inositol 1-phosphate synthase, L-myo-Inositol 1-phosphate synthetase, L-myo-Inositol-1-phosphate synthase, MI-1-P synthase, MIP synthase, MIPS, MIPS1, MIPS2, myo-D-inositol 3-phosphate synthase, myo-inositol 1-phosphate synthase, myo-inositol 3-phosphate synthase, myo-inositol phosphate synthase, myo-Inositol-1-P synthase, Myo-inositol-1-phosphate synthase, myo-inositol-3-phosphate synthase, OsMIPS1, OsMIPS1-1, OsMIPS1-2, OsMIPS1-3, OsMIPS2, PcINO1, PINO1 protein, PIP synthase, PIPS, RINO1 protein, SaINO1, sll1981, Synthase, myo-inositol 1-phosphate, TaMIPS1, TaMIPS2, tbINO, yMIP synthase, [Ins(3)P1] synthase

ECTree

     5 Isomerases
         5.5 Intramolecular lyases
             5.5.1 Intramolecular lyases (only sub-subclass identified to date)
                5.5.1.4 inositol-3-phosphate synthase

Crystallization

Crystallization on EC 5.5.1.4 - inositol-3-phosphate synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, protein solution containing 8 mg/ml or 16 mg/ml protein, 50 mM Tris, pH 7.5, 1 mM EDTA, versus HEPES, pH 7.5, 2% v/v PEG 400, 2.0 M ammonium sulfate, and 30% w/v PEG 1500 in equal volumes, 2-3 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution, modeling
-
hanging-drop vapour-diffusion method, crystal structure of native and selenomethionine-bound enzyme at 1.95 resolution, bound to the cofactor NAD+
-
hanging-drop vapor-diffusion method
-
hanging-drop vapour-diffusion method, selenomethionine-substituted enzyme, 2.65 A crystal structure of recombinant enzyme
-
purified apo-enzyme and in complex with NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate, complexing by soaking of apo-enzyme crystals in 5% PEG 8000, 0.1 M NaAc, pH 5.5, 1 mM NAD+, and 13.5 mM 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate for 24 h, cryoprotection by 30% glycerol, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
structure of the 1L-myo-inositol 1-phosphate synthase/NAD+/2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex
-
structure of the enzyme both completely devoid of NAD+ and completely occupied with NAD+, structure at 1.7 A resolution
-