EC 5.4.2.2 - Phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent)

  IntEnz view ENZYME view
XML

IntEnz Enzyme Nomenclature
EC 5.4.2.2

Names

Accepted name:
phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent)
Other names:
glucose phosphomutase [ambiguous]
phosphoglucose mutase [ambiguous]
Systematic name:
α-D-glucose 1,6-phosphomutase

Reaction

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 5.4.2.5, phosphoglucomutase (glucose-cofactor). Formerly EC 2.7.5.1.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00589
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004614
CAS Registry Number: 9001-81-4
UniProtKB/Swiss-Prot: (66) [show] [UniProt]

References

  1. Joshi, J.G. and Handler, P.
    Phosphoglucomutase. I. Purification and properties of phosphoglucomutase from Escherichia coli.
    J. Biol. Chem. 239 : 2741-2751 (1964).
  2. Najjar, V.A.
    Phosphoglucomutase,
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes , 2nd ed. vol. 6 , Academic Press , New York , 1962 , 161-178
  3. Ray, W.J. and Roscelli, G.A.
    A kinetic study of the phosphoglucomutase pathway.
    J. Biol. Chem. 239 : 1228-1236 (1964).
  4. Ray, W.J., Jr. and Peck, E.J., Jr.
    Phosphomutases,
    In: Boyer, P.D. (Ed.) The Enzymes , 3rd ed. vol. 6 , Academic Press , New York , 1972 , 407-477
  5. Sutherland, E.W., Cohn, M., Posternak, T. and Cori, C.F.
    The mechanism of the phosphoglucomutase reaction.
    J. Biol. Chem. 180 : 1285-1295 (1949).

[EC 5.4.2.2 created 1961 as EC 2.7.5.1, transferred 1984 to EC 5.4.2.2]