EC 184.108.40.206 - Phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent)
IntEnz Enzyme Nomenclature
23536 [IUBMB]α-D-glucose 1-phosphatealpha-D-glucose 1-phosphateName origin: UniProt - CHECKED (C)Formula: C6H11O9P
Charge: -2ChEBI compound status: CHECKED (C)<?>
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 220.127.116.11, phosphoglucomutase (glucose-cofactor). Formerly EC 18.104.22.168.
Links to other databases
Phosphoglucomutase. I. Purification and properties of phosphoglucomutase from Escherichia coli.J. Biol. Chem. 239: 2741-2751 (1964).
Phosphoglucomutase,In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes, 2nd ed. vol. 6, Academic Press, New York, 1962, 161-178
A kinetic study of the phosphoglucomutase pathway.J. Biol. Chem. 239: 1228-1236 (1964).
Phosphomutases,In: Boyer, P.D. (Ed.) The Enzymes, 3rd ed. vol. 6, Academic Press, New York, 1972, 407-477
The mechanism of the phosphoglucomutase reaction.J. Biol. Chem. 180: 1285-1295 (1949).
[EC 22.214.171.124 created 1961 as EC 126.96.36.199, transferred 1984 to EC 188.8.131.52]