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Information on EC 2.7.2.3 - phosphoglycerate kinase and Organism(s) Plasmodium falciparum and UniProt Accession P27362

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Plasmodium falciparum
UNIPROT: P27362 not found.
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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, phosphoglycerate kinase 2, 3-pgk, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-PGK
-
-
-
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3-phosphoglycerate kinase
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-
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3-phosphoglycerate phosphokinase
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-
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3-phosphoglyceric acid kinase
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-
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3-phosphoglyceric acid phosphokinase
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-
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3-phosphoglyceric kinase
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-
-
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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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PGK
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phosphoglyceric acid kinase
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phosphoglyceric kinase
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phosphoglycerokinase
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:3-phospho-D-glycerate 1-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-83-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
key enzyme of anaerobic glycolysis in Plasmodium falciparum
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r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
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
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
key enzyme of anaerobic glycolysis in Plasmodium falciparum
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
required as phosphate donor
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
divalent metal ion required: Ca2+, Mg2+ or Mn2+. Mg2+ is the preferred cation
KCl
-
maximal activation at 100 mM
KH2PO4
-
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
-
maximal activation at 100 mM
NaH2PO4
-
maximal activation at 25-50 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KH2PO4
-
above 50 mM
NaH2PO4
-
above 50 mM
suramin
-
IC50: 0.007 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
-
as Na or K salt continues to activate at concentrations above 200 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52
3-phospho-D-glycerate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
suramin
Plasmodium falciparum
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IC50: 0.007 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
x * 45000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 45000, SDS-PAGE
monomer
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1 * 48000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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30 min, 27% loss of activity
37
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30 min, nearly 80% loss of activity
49
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team