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 (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 (EC5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC5.4.2.12) 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]
^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. PMID17576516. S2CID5836321.
