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Literature summary extracted from

  • Lallemand, P.; Chaloin, L.; Roy, B.; Barman, T.; Bowler, M.W.; Lionne, C.
    Interaction of human 3-phosphoglycerate kinase with its two substrates: is substrate antagonism a kinetic advantage? (2011), J. Mol. Biol., 409, 742-757.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.3 expressed in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.2.3 hPGK crystals are obtained at 20 °C by the sitting drop method. A crystal structure of hPGK in a fully closed conformation in complex with L-ADP, 3-phosphoglycerate, and the transition-state analogue AlF4- is determined Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.2.3 0.077
-
 D-ADP pH 7.5, temperature not specified in the publication Homo sapiens
2.7.2.3 0.1
-
 L-ADP pH 7.5, temperature not specified in the publication Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.3 Homo sapiens P00558
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.3 ADP + 1,3-bisphosphoglycerate using the stopped-flow method it is shown that substrate binding kinetics that lead to the formation of the catalytic PGK-1,3-bisphosphoglycerate-ADP complexes are mutually antagonistic with D-ADP, but much less so with L-ADP. A situation that is similar to that for the formation of the abortive PGK-3-phosphoglycerate-ADP complexes Homo sapiens ATP + 3-phosphoglycerate
-
 ?
2.7.2.3 D-ADP + 1,3-bisphosphoglycerate
-
 Homo sapiens ?
-
 ?
2.7.2.3 L-ADP + 1,3-bisphosphoglycerate with L-ADP, the transient burst phase of ATP is more clear-cut than with D-ADP, suggesting that the product release steps are slower with L-ADP than with D-ADP. This is in accordance with the lower kcat measured with L-ADP compared to D-ADP Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.2.3 3-phosphoglycerate kinase
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.2.3 86
-
 L-ADP pH 7.5, temperature not specified in the publication Homo sapiens
2.7.2.3 200
-
 D-ADP pH 7.5, temperature not specified in the publication Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.3 7.5
-
 assay at Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.2.3 900
-
 L-ADP pH 7.5, temperature not specified in the publication Homo sapiens
2.7.2.3 2600
-
 D-ADP pH 7.5, temperature not specified in the publication Homo sapiens