Literature summary for 5.4.2.11 extracted from

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 (2011), Acta Crystallogr. Sect. F, 67, 1044-1050.

Activating Compound

Activating Compound	Comment	Organism	Structure
2,3-bisphosphoglycerate	dependent on	Burkholderia pseudomallei

Application

Application	Comment	Organism
drug development	as a key enzyme in glycolysis and energy metabolism, PGAM is a potential target for novel antibiotics	Burkholderia pseudomallei

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)-R3-pRARE2 cells	Burkholderia pseudomallei

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Burkholderia pseudomallei

Crystallization (Comment)

Organism

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

Burkholderia pseudomallei

Inhibitors

Inhibitors	Comment	Organism	Structure
vanadate	acting as a substrate mimic, enzyme binding structure, overview	Burkholderia pseudomallei

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2-phospho-D-glycerate	Burkholderia pseudomallei	-	3-phospho-D-glycerate	-	r
2-phospho-D-glycerate	Burkholderia pseudomallei 1710b	-	3-phospho-D-glycerate	-	r

Organism

Organism	UniProt	Comment	Textmining
Burkholderia pseudomallei	Q3JWH7	-	-
Burkholderia pseudomallei 1710b	Q3JWH7	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)-R3-pRARE2 cells by nickel affinity chromatography and gel filtration	Burkholderia pseudomallei

Reaction

Reaction	Comment	Organism	Reaction ID
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	Burkholderia pseudomallei	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-phospho-D-glycerate	-	Burkholderia pseudomallei	3-phospho-D-glycerate	-	r
2-phospho-D-glycerate	-	Burkholderia pseudomallei 1710b	3-phospho-D-glycerate	-	r

Synonyms

Synonyms	Comment	Organism
2,3-bisphosphoglycerate-dependent PGAM	-	Burkholderia pseudomallei
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase	-	Burkholderia pseudomallei

General Information

General Information	Comment	Organism
metabolism	the enzyme catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate as a key step in the glycolytic pathway	Burkholderia pseudomallei
additional information	active site residues are Thr21, Gly22, Tyr90, Lys98, Arg114 and Arg115	Burkholderia pseudomallei