Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
8-oxo-dGTP + H2O | Escherichia coli | - |
8-oxo-dGMP + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
8-oxo-dGTP + H2O | - |
Escherichia coli | 8-oxo-dGMP + diphosphate | - |
? | |
8-oxo-dGTP + H2O | experimental thermodynamic data of 8-oxo-dGMP and dGMP binding to MutT show largely different affinities, even though the difference of chemical structures of the two molecules is very small. Enthalpic and entropic components of the binding free energy suggest drastically different conformational responses of MutT for binding the two molecules. These different conformational responses appear to be the mechanism for the enhanced recognition/discrimination between the two molecules despite a small difference of the chemical structures. Transition between two minimum energy substrates, both existing in the native state of the protein, is involved in high-resolution molecular recognition | Escherichia coli | 8-oxo-dGMP + diphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MutT | - |
Escherichia coli |