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Literature summary extracted from

  • Higuchi, M.; Fujii, J.; Yonetani, Y.; Kitao, A.; Go, N.
    Enhanced resolution of molecular recognition to distinguish structurally similar molecules by different conformational responses of a protein upon ligand binding (2011), J. Struct. Biol., 173, 20-28.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.55 8-oxo-dGTP + H2O Escherichia coli
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 8-oxo-dGMP + diphosphate
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.55 Escherichia coli
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-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.55 8-oxo-dGTP + H2O
-
 Escherichia coli 8-oxo-dGMP + diphosphate
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 ?
3.6.1.55 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
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 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.55 MutT
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 Escherichia coli