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Literature summary for 2.1.1.45 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

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

General Information

General Information Comment Organism
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