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Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)

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IUBMB Comments
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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Synonyms
phosphoglycerate mutase, pgam1, phosphoglycerate mutase 1, sts-1, pgam2, cofactor-dependent phosphoglycerate mutase, dpgm-b, rv3214, 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, b-type pgm, more
REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
2-phospho-D-glycerate = 3-phospho-D-glycerate
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[enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-Ntau-phospho-L-histidine + 2/3-phospho-D-glycerate
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(1a)
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[enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-Ntau-phospho-L-histidine + 3-phospho-D-glycerate
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[enzyme]-Ntau-phospho-L-histidine + 2-phospho-D-glycerate = [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate
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(1b)
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[enzyme]-Ntau-phospho-L-histidine + 2/3-bisphospho-D-glycerate = [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate
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(1d)
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