S
IPR001345

Phosphoglycerate/bisphosphoglycerate mutase, active site

InterPro entry
Short namePG/BPGM_mutase_AS

Description

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, 6]
. 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
[3]
.

A number of other proteins including, the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
[4]
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
[5]
.

This entry contains the active site phosphohistidine residue.

References

1.Molecular cloning and nucleotide sequence of murine 2,3-bisphosphoglycerate mutase cDNA. Le Boulch P, Joulin V, Garel MC, Rosa J, Cohen-Solal M. Biochem. Biophys. Res. Commun. 156, 874-81, (1988). View articlePMID: 2847721

2.Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae. White MF, Fothergill-Gilmore LA. FEBS Lett. 229, 383-7, (1988). View articlePMID: 2831102

3.Intermediates in the phosphoglycerate mutase and bisphosphoglycerate synthase reactions. Rose ZB. Meth. Enzymol. 87, 42-51, (1982). View articlePMID: 6294454

4.Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Bazan JF, Fletterick RJ, Pilkis SJ. Proc. Natl. Acad. Sci. U.S.A. 86, 9642-6, (1989). View articlePMID: 2557623

5.The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin. O'Toole GA, Trzebiatowski JR, Escalante-Semerena JC. J. Biol. Chem. 269, 26503-11, (1994). View articlePMID: 7929373

6.Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase. Jedrzejas MJ. Prog. Biophys. Mol. Biol. 73, 263-87, (2000). View articlePMID: 10958932

GO terms

biological process

  • None

cellular component

  • None

Cross References

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