Phosphoglycerate mutase
| Phosphoglycerate mutase family | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | PGAM | ||||||||
| Pfam | PF00300 | ||||||||
| InterPro | IPR013078 | ||||||||
| PROSITE | PDOC00158 | ||||||||
| SCOP | 3pgm | ||||||||
| SUPERFAMILY | 3pgm | ||||||||
|
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
| phosphoglycerate mutase 1 (brain) | |
|---|---|
 |
|
| Identifiers | |
| Symbol | PGAM1 |
| Alt. symbols | PGAMA |
| Entrez | 5223 |
| HUGO | 8888 |
| OMIM | 172250 |
| RefSeq | NM_002629 |
| UniProt | P18669 |
| Other data | |
| EC number | 5.4.2.11 |
| Locus | Chr. 10 q25.3 |
| phosphoglycerate mutase 2 (muscle) | |
|---|---|
| Identifiers | |
| Symbol | PGAM2 |
| Entrez | 5224 |
| HUGO | 8889 |
| OMIM | 261670 |
| RefSeq | NM_000290 |
| UniProt | P15259 |
| Other data | |
| EC number | 5.4.2.11 |
| Locus | Chr. 7 p13-p12 |
Phosphoglycerate mutase (PGM) is any enzyme that catalyzes step 8 of glycolysis. They catalyze the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase.
PGM is an isomerase enzyme, effectively transferring a phosphate group (PO43−) from the C-3 carbon of 3-phosphoglycerate to the C-2 carbon forming 2-phosphoglycerate. There are a total of three reactions dPGM can catalyze: a mutase reaction resulting in the conversion of 3PG to 2PG and vice versa, a phosphatase reaction creating phosphoglycerate from 2,3-bisphosphoglycerate, and a synthase reaction producing 2,3-bisphosphoglycerate from 1,3-bisphosphoglycerate similar to the enzyme bisphosphoglycerate mutase. Kinetic and structural studies have provided evidence that indicate dPGM and bisphosphoglycerate mutase are paralogous structures. Both enzymes are contained in the superfamily that also contains the phosphatase portion of phosphofructokinase 2 and prostatic acid phosphatase.
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