Open AccessMetabolism of Trehalose in Euglena gracilis
Author(s) -
BELOCOPITOW Enrique,
MARÉCHAL Luis R.
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03659.x
Subject(s) - euglena gracilis , phosphoglucomutase , sephadex , sugar phosphates , trehalose , biochemistry , size exclusion chromatography , chromatography , enzyme , chemistry , biology , euglena , glycogen phosphorylase , phosphate , chloroplast , gene
Phosphoglucomutase for β‐glucose 1‐phosphate, an enzyme present in cell‐free extracts of Euglena gracilis var. bacillaris , catalyzes the reversible conversion of β‐glucose 1‐phosphate to glucose 6‐phosphate. It was purified 460‐fold by treatment with protamine sulphate, gel filtration in Sephadex G‐100 and chromatography on a DEAE‐cellulose column. The optimum pH of the reaction was 7.0 and the equilibrium constant β‐glucose 1‐phosphate/glucose 6‐phosphate was 0.035. The enzyme has an absolute requirement for β‐glucose 1,6‐bisphosphate as well as a bivalent cation such as Mg 2+ , Co 2+ or Mn 2+ . Measurements in Sephadex G‐100 gave an apparent molecular weight of about 27000. This enzyme together with a trehalose phosphorylase found in the same Euglena extracts would constitute a new catabolic pathway for trehalose. The functions of α‐ and β‐glucose 1,6‐bisphosphate as regulation factors in the energy furnisher system in Euglena is discussed.