Literature summary for 2.1.1.45 extracted from

Sobich, J.; Prokopowicz, M.; Maj, P.; Wilk, P.; Zielinski, Z.; Fraczyk, T.; Rode, W.
Thymidylate synthase-catalyzed, tetrahydrofolate-dependent self-inactivation by 5-FdUMP (2019), Arch. Biochem. Biophys., 674, 108106 .

Search for more literature for 2.1.1.45

Inhibitors

Inhibitors	Comment	Organism	Structure
5-fluoro-dUMP	enzyme forms, in the presence of tetrahydrofolate, a covalently bound 5-fluoro-dUMP-thymidylate synthase complex. The tetrahydrofolate- and time-dependent, covalent binding by thymidylate synthase is accompanied by the enzyme inactivation	Mus musculus
N4-hydroxy-dCMP	enzyme forms, in the presence of tetrahydrofolate, a covalently bound 5-fluoro-dUMP-thymidylate synthase complex. The tetrahydrofolate- and time-dependent, covalent binding by thymidylate synthase is accompanied by the enzyme inactivation	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P07607	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)