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2.7.2.3: phosphoglycerate kinase

This is an abbreviated version!
For detailed information about phosphoglycerate kinase, go to the full flat file.

Word Map on EC 2.7.2.3

Reaction

ATP
+
3-phospho-D-glycerate
=
ADP
 +
3-phospho-D-glyceroyl phosphate

Synonyms

3-PGK, 3-phosphoglycerate 1-phosphotransferase, 3-phosphoglycerate kinase, 3-phosphoglycerate phosphokinase, 3-phosphoglyceric acid kinase, 3-phosphoglyceric acid phosphokinase, 3-phosphoglyceric kinase, AbPGK, ATP-3-phospho-D-glycerate-1-phosphotransferase, ATP:3-phospho-D-glycerate 1-phosphotransferase, ATP:D-3-phosphoglycerate 1-phosphotransferase, chl-PGK, glycerate 3-phosphate kinase, glycerophosphate kinase, HacPGK1, HacPGK2, HapPGK, hPGK, HsPGK, human 3-phosphoglycerate kinase, kinase (phosphorylating), phosphoglycerate, Mfer_0156, OsPGK2, P-glycerate kinase, PAS-PGK, PfPGK, PGK, PGK 1, PGK-1, PGK-2, pgk-B, PGK1, PGK2, Pgk3, Pgk5, PGKA, PGKase-1, PGKB, PGKC, pgkp1, pgkp2, phosphoglycerate kinase, phosphoglycerate kinase 1, phosphoglycerate kinase 2, phosphoglycerate kinase B, phosphoglycerate kinase-1, phosphoglyceric acid kinase, phosphoglyceric kinase, phosphoglycerokinase, PwPGK, SjPGK, SSO0527, testis-specific phosphoglycerate kinase 2, TRSC58_02767, X chromosome-linked phosphoglycerate kinase-1

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.2 Phosphotransferases with a carboxy group as acceptor
                2.7.2.3 phosphoglycerate kinase

General Stability

General Stability on EC 2.7.2.3 - phosphoglycerate kinase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin and dithioerythritol stabilize in the enzyme assay
crystalline enzyme is rather unstable, dried crystals or dilute aqueous solutions lose all activity within a few weeks
-
dissolved cyrstallized enzyme at low concentration is rapidly inactivated at neutral pH
-
enzyme shows highest thermal stability in ternary complex with 3-phosphoglycerate and MgADP-, due to domain closure
extensive dialysis against 0.1 M Tris/HCl, pH 7.6, 1 mM DTT, 1 mM EDTA, 1 mM sodium azide, 0.2 M ammonium sulfate, stable
-
freeze-drying inactivates
-
freezing inactivates
-
K+ stabilizes
L-MgADP binds to the specific adenosine-binding site and protects the conformation of hPGK molecule against heat denaturation
-
optimal stabilization at 1 mM EDTA and 5 mM 2-mercaptoethanol
-
phosphoglycerate kinase is resistant to proteolytic cleavage. ecPGK can only be digested through its globally unfolded state, suggesting that cooperativity between the two domains results in a more rigid protein that has low susceptibility to proteolysis
potassium salts of polyvalent anions stabilize the enzyme
Pro204 is important for stability and catalytic mechanism of the enzyme
-
stabilized by anions in decreasing order of efficiency: 2,3-bisphospho-D-glycerate, PO43-, SO42-, Cl-
stable as a suspension in ammonium sulfate, 70-90% saturation
-
the extrapolated unfolding rate of Escherichia coli PGK is 100000 slower than that of the yeast homolog
-
the stabilizing effects of anions on thermal stability