Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and Organism(s) Burkholderia pseudomallei and UniProt Accession Q3JWH7
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The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi 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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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-phospho-D-glycerate = 3-phospho-D-glycerate
mechanism of BPGM begins with an unphosphorylated enzyme, the active site histidine of which performs a nucleophilic SN2 attack on the 1,3-bisphosphoglycerate substrate to produce phosphohistidine and 3-phosphoglycerate. The 2'-hydroxyl group then performs a second nucleophilic attack that transfers the phosphate from the active site histidine to the substrate, forming 2,3-bisphosphoglycerate
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi 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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, in apoform or complexed with 2-phosphoserine, with vanadate + 3-phosphoglycerate, with vanadate + glycerol, with 2,3-bisphosphoglycerate + 3-phosphoglycerate, or with malonate, sitting-drop vapour diffusion by mixing 0.0004 ml reservoir solution with 0.0004 ml protein solution, containing 25 mM HEPES, pH 7.0, 500 mM NaCl, 5% v/v glycerol, 0.025% w/v sodium azide and 2 mM DTT, over a reservoir volume of 0.08 ml, the reservoir solution, containing 5% PEG 1000, 10% glycerol, 30% PEG 600, and 100 mM MES pH 7.5, is supplemented with the ligands at different concentrations, X-ray diffraction structure determination and analysis at 1.5-2.25 A resolution, molecular replacement and modeling