Cloned (Comment) | Organism |
---|---|
overexpressed in the Escherichia coli BL21-CodonPlus (DE3)-RIL | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | deleted T393, substrate binding abilities are hardly changed, but the substrate antagonism, characteristics of the wild-type enzyme, is completely abolished | Homo sapiens |
N336A | substrate binding abilities are hardly changed, but the substrate antagonism, characteristics of the wild-type enzyme, is restricted | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
by sonication | Homo sapiens |
Storage Stability | Organism |
---|---|
-80°C, 50 mM Tris-HCl, 1 mM EDTA buffer, pH 7.5, 1 mM 2-mercaptoethanol | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mg-ADP or Mg-beta,gamma-imido-adenosine 5'-triphosphate substitute the substrate Mg-ATP in the ternary complexes, they cannot react with 3-phospho-D-glyceroyl phosphate. Domain closure and substrate antagonism are closely related phenomena for PGK. Conformational rearrangements in the hinge generated by binding of both substrates provide the main driving force for domain closure overcoming the slightly unfavourable contact interactions between the domains | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
3-phosphoglycerate kinase | - |
Homo sapiens |
PGK | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | in the presence of either beta,gamma-imido-adenosine 5'-triphosphate or ADP binding of 3-phospho-D-glycerate is weakened and the contribution of the entropy-factor to its binding is increased relative to the enthalpy factor | Homo sapiens |