Cytosolic phosphoglucomutase1 (PGM1) catalyses the reversible conversion of glucose 6-phosphate (G6P) to glucose 1-phosphate (G1P) (Drago et al. 1991). Two PGM isoenzymes, both monomers, have been identified which both require Mg2+ as cofactor. PGM1 is the major form found in most tissues except erythrocytes, where PGM2 is abundant (March et al. 1993; Parrington et al. 1968; Putt et al. 1993). PGM2 also has substantial phosphopentomutase activity (Maliekal et al. 2007) and its primary physiological in normal tissues in vivo is not clear. Cytosolic glucose 1,6-bisphosphate synthase (PGM2L1) also possesses phosphoglucomutase activity (Maliekal et al. 2007, Veiga-da-Cunha et al. 2008).
Veiga-da-Cunha, M, Vleugels, W, Maliekal, P, Matthijs, G, Van Schaftingen, E
March, RE, Putt, W, Hollyoake, M, Ives, JH, Lovegrove, JU, Hopkinson, DA, Edwards, YH, Whitehouse, DB
Maliekal, P, Sokolova, T, Vertommen, D, Veiga-da-Cunha, M, Van Schaftingen, E
Drago, GA, Hopkinson, DA, Westwood, SA, Whitehouse, DB
Putt, W, Ives, JH, Hollyoake, M, Hopkinson, DA, Whitehouse, DB, Edwards, YH
phosphoglucomutase activity of PGM1:Mg2+ [cytosol]
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