Literature summary for 3.6.1.55 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.

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Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
MutT	-	Escherichia coli

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Release 2023.1 (January 2023)