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Literature summary for 2.7.2.3 extracted from

  • Varga, A.; Lionne, C.; Lallemand, P.; Szabo, J.; Adamek, N.; Valentin, C.; Vas, M.; Barman, T.; Chaloin, L.
    Direct kinetic evidence that lysine 215 is involved in the phospho-transfer step of human 3-phosphoglycerate kinase (2009), Biochemistry, 48, 6998-7008.
    View publication on PubMed
Search for more literature for 2.7.2.3

Protein Variants

Protein Variants Comment Organism
K215A kinetics of substrate binding and the associated protein isomerization steps are fast and identical for the wild-type and mutant K215A. Has a low inherent phosphotransferase activity, with the mutant the conserved Arg 65 replaces the missing Lys 215 by helping to position the transferable phospho group during the reaction. In the mutant the closed conformation of the enzyme is stabilized by a salt bridge between Asp 218 and Arg 170 rather than Arg 65 in the wild-type PGK Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
 ATP wild-type, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
0.077
-
 ADP wild-type, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
0.126
-
 ADP mutant K215A, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
1.6
-
 ATP mutant K215A, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-phospho-D-glycerate
-
 Homo sapiens ADP + 3-phospho-D-glyceroyl 1-phosphate
-
 r
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
 Homo sapiens ATP + 3-phospho-D-glycerate
-
 r

Synonyms

Synonyms Comment Organism
3-phosphoglycerate kinase
-
 Homo sapiens
PGK
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
 ATP mutant K215A, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
0.06
-
 ADP mutant K215A, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
0.48
-
 ATP mutant K215A, at 20°C, in methanol-free buffer, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
0.78
-
 ADP mutant K215A, at 20°C, in methanol-free buffer, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
2.48
-
 ATP wild-type, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
200
-
 ADP wild-type, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
833
-
 ATP wild-type, at 20°C, in methanol-free buffer, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
2633
-
 ADP wild-type, at 20°C, in methanol-free buffer, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.03
-
 ATP mutant K215A, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
0.48
-
 ADP mutant K215A, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
150
-
 ATP wild-type, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens
2600
-
 ADP wild-type, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+ Homo sapiens