Phosphoglycerate mutase

Citrate is structurally similar to the substrate 3-phosphoglycerate. The citrate molecule is shown in green. The suspected catalytically essential histidine residue involved in forming the phosphohistidine complex is directly to the left of the bound citrate molecule.
Phosphoglycerate mutase family
Identifiers
SymbolPGAM
PfamPF00300
InterProIPR013078
PROSITEPDOC00158
SCOP23pgm / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1e59A:5-191 1e58A:5-191 1yjxD:5-193

1yfkA:5-193 1ljdA:5-193 1fztA:9-170 4pgmB:3-189 3pgmB:3-189 1qhfA:3-189 1bq3B:3-189 1bq4B:3-189 1riiA:6-190 1t8pA:5-195 1h2eA:2-151 1h2fA:2-151 1ebbA:2-151 2bifA:251-398 3bifA:251-398 1bif :251-398 1k6mB:253-400 1c80A:253-400 1c7zA:253-400 1fbtB:253-400 1c81A:253-400

2axnA:248-395 1ujcA:2-115 1ujbA:2-115
phosphoglycerate mutase 1 (brain)
Identifiers
SymbolPGAM1
Alt. symbolsPGAMA
NCBI gene5223
HGNC8888
OMIM172250
RefSeqNM_002629
UniProtP18669
Other data
EC number5.4.2.11
LocusChr. 10 q25.3
Search for
StructuresSwiss-model
DomainsInterPro
phosphoglycerate mutase 2 (muscle)
Identifiers
SymbolPGAM2
NCBI gene5224
HGNC8889
OMIM261670
RefSeqNM_000290
UniProtP15259
Other data
EC number5.4.2.11
LocusChr. 7 p13-p12
Search for
StructuresSwiss-model
DomainsInterPro
This enzyme is not to be confused with Bisphosphoglycerate mutase which catalyzes the conversion of 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate.

Phosphoglycerate mutase (PGM) is any enzyme that catalyzes step 8 of glycolysis - 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).[1] 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.[2] This class of PGM enzyme shares the same superfamily as alkaline phosphatase.[3]

  1. ^ Johnsen, U; Schönheit, P (September 2007). "Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea". Extremophiles: Life Under Extreme Conditions. 11 (5): 647–57. doi:10.1007/s00792-007-0094-x. PMID 17576516. S2CID 5836321.
  2. ^ Jedrzejas, MJ (2000). "Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase". Progress in Biophysics and Molecular Biology. 73 (2–4): 263–87. doi:10.1016/s0079-6107(00)00007-9. PMID 10958932.
  3. ^ Galperin, MY; Bairoch, A; Koonin, EV (August 1998). "A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases". Protein Science. 7 (8): 1829–35. doi:10.1002/pro.5560070819. PMC 2144072. PMID 10082381.

© MMXXIII Rich X Search. We shall prevail. All rights reserved. Rich X Search