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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 3-phospho-D-glycerate | - |
Homo sapiens | ADP + 3-phospho-D-glyceroyl phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
human 3-phosphoglycerate kinase | - |
Homo sapiens |
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 |