cd16010

2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM

CDD entry
Member databaseCDD
CDD typedomain
Short nameiPGM
SetALP_like

Description

The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
[3, 4, 2, 5, 1, 6]

References

1.Structure and mechanism of alkaline phosphatase. Coleman JE. 21, 441-83, (1992). View articlePMID: 1525473

2.Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus. Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G. EMBO J. 19, 1419-31, (2000). View articlePMID: 10747010

3.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

4.Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate. Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G. J. Biol. Chem. 275, 23146-53, (2000). View articlePMID: 10764795

5.Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus. Chander M, Setlow P, Lamani E, Jedrzejas MJ. J. Struct. Biol. 126, 156-65, (1999). View articlePMID: 10388626

6.A revised mechanism for the alkaline phosphatase reaction involving three metal ions. Stec B, Holtz KM, Kantrowitz ER. J. Mol. Biol. 299, 1303-11, (2000). View articlePMID: 10873454

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