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5.4.2.2: phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)

This is an abbreviated version!
For detailed information about phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent), go to the full flat file.

Word Map on EC 5.4.2.2

Reaction

alpha-D-glucose 1-phosphate
=
D-glucose 6-phosphate

Synonyms

alpha phosphoglucomutase, alpha-Pgm, alpha-phosphoglucomutase, alpha-phosphoglucomutase 1, alpha-phosphoglucose mutase, cPGM, cytosolic phosphoglucomutase, EC 2.7.5.1, Glucose phosphomutase, PGM, PGM-I, PGM-II, PGM/PMM, PGM1, PGM2, PGM3, PgmA, PgmG, phospho-glucomutase, phosphoglucomutase, phosphoglucomutase 1, phosphoglucomutase/phosphomannomutase, phosphoglucomutase1, Phosphoglucose mutase, Phosphohexomutase, phosphomannomutase/phosphoglucomutase, Phosphomutase, glucose, plastidic phosphoglucomutase, PMM/PGM, pPGM, SP-1, SpgM, SSO0207, XanA, YMR278w protein

ECTree

     5 Isomerases
         5.4 Intramolecular transferases
             5.4.2 Phosphotransferases (phosphomutases)
                5.4.2.2 phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)

Crystallization

Crystallization on EC 5.4.2.2 - phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, mutant enzyme D263Y crystals grow in solutions including lithium or ammonium sulfate (1.4-1.55 M) with 0.1 M buffer of either MES, pH 6.0, or Tris HCl, pH 7.5. Crystals of mutant enzyme D263G grow from 1.6 M ammonium sulfate, 0.1 M NaCl, and 0.1 M HEPES, pH 7.5
crystallized with vapor diffusion, streak seeding, in ammonium sulfate solution, optimized crystals diffract to 1.5 A resolution
hanging drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.0, 10% (w/v) PEG 3350, 10 mM MgCl2 and 0.02% (w/v) NaN3
crystal structure at 2.7 A resolution
-
crystallization procedure, polyethyleneglycol-400, 1-4.5% must be included in crystal growth medium
-
production of active enzyme-substrate/product complexes
-
hanging drop vapor diffusion, 12-15 mg/ml PMM/PGM in 10 mM MOPS, pH 7.0, 1.4 M sodium/potassium tartrate and 100 mM Na-HEPES, pH 7.5, crystals diffract to 1.75 A resolution
-
in complex with inhibitor xylose 1-phosphate or slow substrate ribose 1-phosphate. Both ligands induce an interdomain rearrangement, using different enzyme-ligand interactions
-
phospho- and dephospho-enzyme in complex with reaction intermediate glucose 1,6-bisphosphate at 1.9 and 2.0 A
-
purified recombinant detagged enzyme, hanging drop vapor diffusion and microseeding techniques, 1.3 to 1.4 M sodium/potassium tartrate and 100 mM HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
-
purified recombinant untagged enzyme mutant H329A, from 1.2-1.6 M Na,K tartrate and 100 mM Na HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
-
hanging drop vapor diffusion method, using 0.1 M Bis-Tris, pH 6.5, 0.2 M MgCl2, and 25% (w/v) PEG 3350
vapor diffusion method, using 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% 2-methyl-2,4-pentanediol, 30 mM MgCl2, 30 mM CaCl2 and 100 mM MOPS/HEPES pH 7.5