Metabolism of glucose 1,6-P2--III. Partial purification and characterization of glucose 1,6-P2 synthase from pig skeletal muscle.
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. 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. Both glucose 1-P and glucose 6-P can act as acceptors of the phosphoryl group from glycerate 1,3-P2. 4. The Km values are 19 microM and 67 nM for glucose 1-P and glycerate 1,3-P2, respectively. 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.
Carreras
M
M
Departament de Ciències Fisiològiques Humanes i de la Nutrició, Facultat de Medicina, Universitat de Barcelona, Spain.
Carreras
J
J
Climent
F
F
D000818:Animals; D004163:Diphosphoglyceric Acids / Q000494:pharmacology; D019298:Glucose-6-Phosphate / Q000031:analogs & derivatives*; D005958:Glucosephosphates / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000378:metabolism*; D010770:Phosphotransferases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D013552:Swine
D004163:Diphosphoglyceric Acids; D005958:Glucosephosphates; C015891:glycerate 1,3-biphosphate; D019298:Glucose-6-Phosphate; C016473:glucose-1,6-bisphosphate; D010770:Phosphotransferases; C020583:glucose 1,6-bisphosphate synthase