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5.3.1.9: glucose-6-phosphate isomerase

This is an abbreviated version!
For detailed information about glucose-6-phosphate isomerase, go to the full flat file.

Word Map on EC 5.3.1.9

Reaction

alpha-D-glucose 6-phosphate
=
beta-D-fructofuranose 6-phosphate

Synonyms

6-Phosphoglucose isomerase, AfcPGI, AMF, AMF/PGI, At4g24620, autocrine motility factor, autocrine motility factor/phosphoglucose isomerase, Cupin-PGI, D-Glucose-6-phosphate isomerase, D-glucose-6-phosphate ketol-isomerase, G6-PI, Glucose 6-phosphate isomerase, Glucose phosphate isomerase, Glucose phosphoisomerase, glucose-6-phosphate isomerase, glucose-6-phosphate isomerase, cytosolic, Glucosephosphate isomerase 2, GPI, Hexose 6-phosphate isomerase, Hexose isomerase, Hexose monophosphate isomerase, Hexose phosphate isomerase, Hexosephosphate isomerase, Isomerase, glucose phosphate, Neuroleukin, NLK, Oxoisomerase, PGI, PGI/AMF, Pgi1, PGI2, PGI3, pgiA, PHI, Phosphoglucoisomerase, Phosphoglucose isomerase, phosphoglucose isomerase/autocrine motility factor, Phosphohexoisomerase, Phosphohexomutase, Phosphohexose isomerase, Phosphosaccharomutase, SA-36, Sperm antigen-36, SwoM, TK1111, VEG54, Vegetative protein 54

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.1 Interconverting aldoses and ketoses, and related compounds
                5.3.1.9 glucose-6-phosphate isomerase

Crystallization

Crystallization on EC 5.3.1.9 - glucose-6-phosphate isomerase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal strcuture at 2.3 A resolution
hanging drop vapor diffusion method, crystal structure of the enzyme complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5 A and 2.3 A resolution, respectively. The inhibitors bind to a region within the domains interface and interact with His306 from the other subunit
molecular modeling and dynamics simulation of GTP binding
-
native enzyme and enzyme lacking N-terminal 47 amino acids. Comparison of data with mammalian enzymes
-
native enzyme and in complex with glucose 6-phosphate or erythrose 4-phosphate
hanging drop vapor diffusion method, using 1.2 M ammonium sulfate pH 8.5 (0.1 M HEPES) and 5% (v/v) glycerol at 10°C
resolution of 2.8 A, space group I212121
-
enzyme complexed with the competitive inhibitor D-gluconate 6-phosphate, X-ray crystallography at 2.5 A resolution
hanging drop vapor diffusion method, X-ray crystal structure of the enzyme complexed with the cyclic form of its substrate, D-fructose 6-phosphate, at 2.1 A resolution
in complex with D-sorbitol 6-phosphate
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing 0.002 ml of both protein solution and reservoir solution, the latter containing 38% v/v PEG 400 and 0.2 M calcium acetate in 0.1 M sodium cacodylate-HCl, pH 6.5, equilibration over 0.5 ml of reservoir solution, 1 week, X-ray diffraction structure determination and analysis at 1.5 A resolution
-
both in complex with fructose 6-phosphate and with glucose 6-phosphate
both native form and in complex with 5-phosphoarabinonate
1.9 A resolution, crystals belong to the space group P2(1)
hanging-drop method of vapour diffusion using 1.6 M sodium citrate as the precipitant at pH 6.5. Maximum resolution of 1.92 A on a single selenomethionine-incorporated crystal. Crystal belongs to space group C2, with approximate unit-cell parameters a = 84.7, b = 42.4, c = 57.3 A, beta = 120.6° and a monomer in the asymmetric unit
-
in presence of bound zinc, substrate D-fructose 6-phosphate and several competitive inhibitors
native form and in comlex with 5-phospho-D-arabinonate, in presence and absence of Mn2+
structure is determined by X-ray diffraction to 2 A resolution
-
vapor diffusion using the hanging drop method, crystal structure of the enzyme in native form and in complex with two active site ligands, 5-phosphoarabinonate and gluconate 6-phosphate
enzyme complexed with glucose 6-phosphate, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
purified recombinant His-tagged enzyme complexed with glucose 6-phosphate, by hanging drop vapor diffusion method at room temperature, 0.004 ml of protein solution with 28.4 mg/ml protein and 5 mM fructose 6-phosphate is mixed with 0.002 ml of reservoir solution containing 10% PEG 3350, 50 mM sodium citrate, and 50 mM dithiothreitol, a few days, X-ray diffraction structure determination and analysis at 1.6 A resolution. Although fructose 6-phosphate is added to the crystallization mixture, the enzyme shows bound gluose 6-phosphate at its active site in the crystals