For diagram click here.
Other name(s): glucose phosphomutase (ambiguous); phosphoglucose mutase (ambiguous)
Systematic name: α-D-glucose 1,6-phosphomutase
Comments: Maximum activity is only obtained in the presence of α-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other α-D-hexoses, and the interconversion of α-D-ribose 1-phosphate and 5-phosphate. cf. EC 18.104.22.168, phosphoglucomutase (glucose-cofactor).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-81-4
1. Joshi, J.G. and Handler, P. Phosphoglucomutase. I. Purification and properties of phosphoglucomutase from Escherichia coli. J. Biol. Chem. 239 (1964) 2741-2751. [PMID: 14216423]
2. Najjar, V.A. Phosphoglucomutase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 6, Academic Press, New York, 1962, pp. 161-178.
3. Ray, W.J. and Roscelli, G.A. A kinetic study of the phosphoglucomutase pathway. J. Biol. Chem. 239 (1964) 1228-1236.
4. Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases, in Boyer, P.D. (Ed.), The Enzymes, 3rd edn., vol. 6, Academic Press, New York , 1972, pp. 407-477.
5. Sutherland, E.W., Cohn, M., Posternak, T. and Cori, C.F. The mechanism of the phosphoglucomutase reaction. J. Biol. Chem. 180 (1949) 1285-1295.