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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)

General Stability

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

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at pH 7.5, the PGM activity in the HEPES buffer is 20% lower than in the Tris-HCl buffer
-
extremely unstable in crude extracts, protease sensitive, Bacillus subtilis 168 SR 22 can be used as a protease-negative mutant
-
freezing and thawing results in almost total loss of activity, freeze-dried enzyme stable
-
loss of activity is observed when phosphate buffer is used in the pH range of 6.0-8.0
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stable in 5 mM acetate buffer or 10 mM citrate buffer, pH 5.5, 4 C, but in 5 mM Tris-HCl buffer pH 7.4, 80% loss of activity per day
-