Phosphoglycerate mutase (5.4.2.1) (PGAM) and bisphosphoglycerate mutase (5.4.2.4) (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate [1, 2, 3]. Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase 3.1.3.13 activity).

In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.

BPGM is a dimeric protein and is found mainly in erythrocytes where it plays a major role in regulating haemoglobin oxygen affinity as a consequence of controlling 2,3-DPG concentration. The catalytic mechanism of both PGAM and BPGM involves the formation of a phosphohistidine intermediate [4].

A number of other proteins including, the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase [5] that catalyses both the synthesis and the degradation of fructose-2,6-bisphosphate and bacterial alpha-ribazole-5'-phosphate phosphatase, which is involved in cobalamin biosynthesis, belong to this family [6].

This entry contains the active site phosphohistidine residue.

1. Molecular cloning and nucleotide sequence of murine 2,3-bisphosphoglycerate mutase cDNA. Biochem. Biophys. Res. Commun. 156, 874-81
2. Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae. FEBS Lett. 229, 383-7
3. Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase. Prog. Biophys. Mol. Biol. 73, 263-87
4. Intermediates in the phosphoglycerate mutase and bisphosphoglycerate synthase reactions. Meth. Enzymol. 87, 42-51
5. Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Proc. Natl. Acad. Sci. U.S.A. 86, 9642-6
6. The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin. J. Biol. Chem. 269, 26503-11

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