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Metabolism of glucose 1,6-P2—III. Partial purification and characterization of glucose 1,6-P2 synthase from pig skeletal muscle

Departament de Ciéncies Fisiológiques Humanes i de la Nutrició (Bioquímica), Facultat de Medicina, Universitat de Barcelona, Casanova 143, 08036-Barcelona, Spain
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry DOI: 10.1016/0305-0491(88)90328-8

ABSTRACT 1.1. Glycerate 1,3-P2-dependent glucose, 1,6-P2 synthase has been purified 2000-fold from pig skeletal muscle, with a yield of 75%.2.2. The enzyme possesses fructose 1,6-P2-dependent glucose 1,6-P2 synthase and phosphoglucomutase activities, which represent 0.1 and 60% of the main activity, respectively.3.3. Both glucose 1-P and glucose 6-P can act as acceptors of the phosphoryl group from glycerate 1,3-P2.4.4. The values are 19 μM and 67 nM for glucose 1-P and glycerate 1,3-P2, respectively.5.5. The enzyme is inhibited by glycerate 2,3-P2, fructose 1,6-P2, glycerate 3-P, phosphoenolpyruvate and lithium, the inhibition pattern varying with the compound.

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