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Literature summary for 2.7.2.3 extracted from

  • Varga, A.; Palmai, Z.; Gugolya, Z.; Graczer, E.; Vonderviszt, F.; Zavodszky, P.; Balog, E.; Vas, M.
    Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase (2012), Biochemistry, 51, 10197-10207.
    View publication on PubMed
Search for more literature for 2.7.2.3

Protein Variants

Protein Variants Comment Organism
D218A binding of both Mg-free ADP and ATP stronger in the following order: mutant D218A inferiour to mutant D374A inferiour to mutant D218A/D374A. Mutations of D218 or D374 strengthen the binding of MgADP and MgATP to the open conformation of 3-phosphoglycerate kinase. Km (MgATP) similar to wild-type, Km (L-aspartate) increased compared to wild-type, kcat decreased compared to wild-type. Km (Mg2+) increased 3fold compared to wild-type Homo sapiens
D218A/D374A binding of both Mg-free ADP and ATP stronger in the following order: mutant D218A inferiour to mutant D374A inferiour to mutant D218A/D374A. Mutations of D218 or D374 strengthen the binding of MgADP and MgATP to the open conformation of 3-phosphoglycerate kinase. Km (MgATP) increased compared to wild-type, Km (L-aspartate) increased compared to wild-type, kcat decreased compared to wild-type. Km (Mg2+) increased 10fold compared to wild-type Homo sapiens
D374A binding of both Mg-free ADP and ATP stronger in the following order: mutant D218A inferiour to mutant D374A inferiour to mutant D218A/D374A. Mutations of D218 or D374 strengthen the binding of MgADP and MgATP to the open conformation of 3-phosphoglycerate kinase. Km (MgATP) and Km (L-aspartate) similar to wild-type, kcat similar to wild-type. Km (Mg2+) increased 8fold compared to wild-type Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
 3-phospho-D-glycerate wild-type, pH and temperature not specified in the publication Homo sapiens
0.11
-
 ATP wild-type, pH and temperature not specified in the publication Homo sapiens
0.11
-
 ATP mutant D218A, pH and temperature not specified in the publication Homo sapiens
0.12
-
 3-phospho-D-glycerate mutant D374A, pH and temperature not specified in the publication Homo sapiens
0.18
-
 ATP mutant D374A, pH and temperature not specified in the publication Homo sapiens
0.2
-
 ATP mutant D218A/D374A, pH and temperature not specified in the publication Homo sapiens
0.24
-
 3-phospho-D-glycerate mutant D218A/D374A, pH and temperature not specified in the publication Homo sapiens
0.27
-
 3-phospho-D-glycerate mutant D218A, pH and temperature not specified in the publication Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
human 3-phosphoglycerate kinase
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13.5
-
 3-phospho-D-glycerate co-substrate: ATP, mutant D218A/D374A, pH and temperature not specified in the publication Homo sapiens
100
-
 3-phospho-D-glycerate co-substrate: ATP, mutant D218A, pH and temperature not specified in the publication Homo sapiens
208
-
 3-phospho-D-glycerate co-substrate: ATP, mutant D374A, pH and temperature not specified in the publication Homo sapiens
220
-
 3-phospho-D-glycerate co-substrate: ATP, wild-type, pH and temperature not specified in the publication Homo sapiens