Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 3-phospho-D-glycerate | Homo sapiens | - |
ADP + 3-phospho-D-glyceroyl phosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P00558 | gene PGK1 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 3-phospho-D-glycerate | - |
Homo sapiens | ADP + 3-phospho-D-glyceroyl phosphate | - |
r |
Synonyms | Comment | Organism |
---|---|---|
3-phosphoglycerate 1-phosphotransferase | - |
Homo sapiens |
PGK1 | - |
Homo sapiens |
phosphoglycerate kinase 1 | - |
Homo sapiens |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
5 | 8 | hPGK1 remains in a native conformation at pH 5-8, but undergoes a conformational transition to a molten globule-like state at acidic pH. hPGK1 kinetic stability remains essentially constant at pH 6-8, but is significantly reduced when pH is decreased from pH 6 to pH 5 | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | mutations in hPGK1 cause human PGK1 deficiency, a rate metabolic conformational disease. Most of these mutations cause protein kinetic destabilization by significant changes in the structure/energetics of the transition state for irreversible denaturation. Protein kinetic destabilization by acidic pH is strongly linked to lower thermodynamic stability, while in disease-causing mutations seems to be linked to lower unfolding cooperativity. The plasticity of the hPGK1 denaturation mechanism responds differently to changes in pH and in disease-causing mutations | Homo sapiens |
additional information | protein conformation, thermodynamic and kinetic stability in hPGK1, overview. pH-Dependent linkage between decreased thermal kinetic stability and thermodynamic stability. hPGK1 remains in a native conformation at pH 5-8, but undergoes a conformational transition to a molten globule-like state at acidic pH. hPGK1 kinetic stability remains essentially constant at pH 6-8, but is significantly reduced when pH is decreased from pH 6 to pH 5. This decrease in kinetic stability is caused by significant changes in the energetic/structural balance of the denaturation transition state, which diverge from those found for disease-causing mutations. Protein kinetic destabilization by acidic pH is strongly linked to lower thermodynamic stability, while in disease-causing mutations seems to be linked to lower unfolding cooperativity. The plasticity of the hPGK1 denaturation mechanism responds differently to changes in pH and in disease-causing mutations | Homo sapiens |
physiological function | human phosphoglycerate kinase 1 is a glycolytic enzyme essential for ATP synthesis, and it is implicated in different pathological conditions such as inherited diseases, oncogenesis and activation of drugs for cancer and viral treatments. Enzyme PGK catalyzes the reversible phosphotransfer from ATP to 3-phosphoglycerate yielding ADP and 1,3-biphosphoglycerate, an essential step for ATP synthesis in the glycolytic pathway | Homo sapiens |