phosphoglycerate mutase;
phosphoglycerate phosphomutase;
phosphoglyceromutase;
glycerate phosphomutase (diphosphoglycerate cofactor);
monophosphoglycerate mutase;
monophosphoglyceromutase;
diphosphoglycomutase;
diphosphoglycerate mutase;
bisphosphoglyceromutase;
GriP mutase;
MPGM;
PGA mutase;
PGAM-i;
PGAM;
PGAM-d;
PGM

Isomerases;
Intramolecular transferases;
Phosphotransferases (phosphomutases)

D-phosphoglycerate 2,3-phosphomutase

2-phospho-D-glycerate = 3-phospho-D-glycerate [RN:R01518]

R01518;
(other) R01662

2-phospho-D-glycerate [CPD:C00631]

The enzymes from mammals and from yeast are phosphorylated by (2R)-2,3-bis-phosphoglycerate, which is also an intermediate (see introduction to section EC 5.4.2). With the rabbit muscle enzyme, dissociation of bisphosphate from the enzyme is much slower than the overall isomerization. These enzymes also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase; they were formerly listed as EC 2.7.5.3. Enzymes from wheat, rice, insects and some fungi, however, have maximum activity in the absence of 2,3-bisphosphoglycerate, and were formerly listed under the present number as phosphoglycerate phosphomutase.