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Literature summary extracted from

  • Sapienza, P.J.; Falk, B.T.; Lee, A.L.
    Bacterial thymidylate synthase binds two molecules of substrate and cofactor without cooperativity (2015), J. Am. Chem. Soc., 137, 14260-14263 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.45 5F-dUMP mechanism-based inhibitor Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.45 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.45 5,10-methylenetetrahydrofolate + dUMP
-
 Escherichia coli dihydrofolate + dTMP
-
 ?

General Information

EC Number General Information Comment Organism
2.1.1.45 physiological function the nucleotide binds to the free and singly bound forms of the enzyme with nearly equal affinity over a broad range of temperatures and in multiple buffers. There are small but significant differences in DELTACP for the two binding event, so the active sites are not formally equivalent. There is little-to-no allostery at the level of DELTAGbind. There is minor inter-subunit cooperativity in formation of a ternary complex with the mechanism-based inhibitor, 5F-dUMP, and cofactor Escherichia coli