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Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and Organism(s) Burkholderia pseudomallei and UniProt Accession Q3JWH7

for references in articles please use BRENDA:EC5.4.2.11
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EC Tree
IUBMB Comments
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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Burkholderia pseudomallei
UNIPROT: Q3JWH7
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The taxonomic range for the selected organisms is: Burkholderia pseudomallei
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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[enzyme]-L-histidine
+
2,3-bisphospho-D-glycerate
=
[enzyme]-Ntau-phospho-L-histidine
+
3-phospho-D-glycerate
[enzyme]-L-histidine
+
=
[enzyme]-Ntau-phospho-L-histidine
+
2-phospho-D-glycerate
=
3-phospho-D-glycerate
=
Synonyms
phosphoglycerate mutase, pgam1, phosphoglycerate mutase 1, sts-1, pgam2, cofactor-dependent phosphoglycerate mutase, dpgm-b, bisphosphoglycerate phosphatase, 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, rv3214, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,3-bisphosphoglycerate-dependent PGAM
-
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-phospho-D-glycerate = 3-phospho-D-glycerate
show the reaction diagram
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
SYSTEMATIC NAME
IUBMB Comments
D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-dependent)
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
-
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
vanadate
acting as a substrate mimic, enzyme binding structure, overview
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
dependent on
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate as a key step in the glycolytic pathway
additional information
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)-R3-pRARE2 cells by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)-R3-pRARE2 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
as a key enzyme in glycolysis and energy metabolism, PGAM is a potential target for novel antibiotics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Davies, D.R.; Staker, B.L.; Abendroth, J.A.; Edwards, T.E.; Hartley, R.; Leonard, J.; Kim, H.; Rychel, A.L.; Hewitt, S.N.; Myler, P.J.; Stewart, L.J.
An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Acta Crystallogr. Sect. F
67
1044-1050
2011
Burkholderia pseudomallei (Q3JWH7), Burkholderia pseudomallei, Burkholderia pseudomallei 1710b (Q3JWH7)
Manually annotated by BRENDA team