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EC Tree
The taxonomic range for the selected organisms is: Plasmodium falciparum The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pgk, phosphoglycerate kinase, pgk-1, 3-phosphoglycerate kinase, phosphoglycerate kinase 1, pgk-2, phosphoglycerate kinase-1, phosphoglycerokinase, 3-pgk, phosphoglycerate kinase 2,
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3-phosphoglycerate kinase
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3-phosphoglycerate phosphokinase
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3-phosphoglyceric acid kinase
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3-phosphoglyceric acid phosphokinase
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3-phosphoglyceric kinase
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ATP-3-phospho-D-glycerate-1-phosphotransferase
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ATP:D-3-phosphoglycerate 1-phosphotransferase
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glycerate 3-phosphate kinase
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glycerophosphate kinase
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kinase (phosphorylating), phosphoglycerate
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phosphoglyceric acid kinase
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phosphoglyceric kinase
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phosphoglycerokinase
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phospho group transfer
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
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key enzyme of anaerobic glycolysis in Plasmodium falciparum
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r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
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r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
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?
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ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
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key enzyme of anaerobic glycolysis in Plasmodium falciparum
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r
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ATP
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required as phosphate donor
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Ca2+
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divalent metal ion required: Ca2+, Mg2+ or Mn2+. Mg2+ is the preferred cation
KCl
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maximal activation at 100 mM
KH2PO4
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maximal activation at 25-50 mM
Mg2+
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divalent metal ion required: Ca2+, Mg2+ or Mn2+. Mg2+ is the preferred cation. Optimal concentration of Mg2+ is 5-15 mM
Mn2+
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divalent metal ion required: Ca2+, Mg2+ or Mn2+. Mg2+ is the preferred cation
NaCl
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maximal activation at 100 mM
NaH2PO4
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maximal activation at 25-50 mM
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acetate
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as Na or K salt continues to activate at concentrations above 200 mM
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0.52
3-phospho-D-glycerate
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0.007
suramin
Plasmodium falciparum
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IC50: 0.007 mM
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UniProt
brenda
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45000
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x * 45000, SDS-PAGE
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monomer
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1 * 48000, SDS-PAGE
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crystal structures of Plasmodium falciparum phosphoglycerate kinase (PfPGK) is determined in open conformation in two different crystal forms to 2.7 A and 3 A resolution, respectively. In both structures a sulfate ion is bound in the ATP binding site and a second sulfate ion is located at the regulatory basic patch in the second crystal form
hanging-drop vapour-diffusion method, recombinant enzyme forms a hexagonal space group P6(1)22 with unit cell parameters a = b = 140.7 A, c = 263.9 A, 3.0 A resolution
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25
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30 min, 27% loss of activity
37
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30 min, nearly 80% loss of activity
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30 min, approximately 95% loss of activity
61
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30 min, enzyme retains less than 4% of its activity
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using Ni-NTA chromatography
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expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
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Grall, M.; Srivastava, I.K.; Schmidt, M.; Garcia, A.M.; Mauel, J.; Perrin, L.H.
Plasmodium falciparum: identification and purification of the phosphoglycerate kinase of the malaria parasite
Exp. Parasitol.
75
10-18
1992
Plasmodium falciparum
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Pal, B.; Pybus, B.; Muccio, D.D.; Chattopadhyay, D.
Biochemical characterization and crystallization of recombinant 3-phosphoglycerate kinase of Plasmodium falciparum
Biochim. Biophys. Acta
1699
277-280
2004
Plasmodium falciparum
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Smith, C.D.; Chattopadhyay, D.; Pal, B.
Crystal structure of Plasmodium falciparum phosphoglycerate kinase: evidence for anion binding in the basic patch
Biochem. Biophys. Res. Commun.
412
203-206
2011
Plasmodium falciparum (P27362), Plasmodium falciparum
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