Literature summary extracted from

Alexandrova, L.A.; Chekhov, V.O.; Shmalenyuk, E.R.; Kochetkov, S.N.; El-Asrar, R.A.; Herdewijn, P.
Synthesis and evaluation of C-5 modified 2-deoxyuridine monophosphates as inhibitors of M. tuberculosis thymidylate synthase (2015), Bioorg. Med. Chem., 23, 7131-7137.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.1.1.148	molecular modeling of the complex with inhibitor 5-undecyloxymethyl-2'-deoxyuridine 5'-monophosphate. Inhibitor contacts mainly with amino acid residues of subunits A and C. The hydrophobic substituent at the C-5 position of nucleic base occupies active site mainly due to lipophilic interactions. Several amino acids of the active site such as Arg95, Gln103, Arg107, Arg172, and Gln106 being involved in the interaction with natural substrate dUMP contribute for affinity due to hydrogen bonds	Mycobacterium tuberculosis

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.1.1.148	5-undecyloxymethyl-2'-deoxyuridine 5'-monophosphate	no activity against classical thymidylate synthase ThyA, EC 2.1.1.45	Mycobacterium tuberculosis

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.1.148	Mycobacterium tuberculosis	-	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
2.1.1.148	ThyX	-	Mycobacterium tuberculosis

IC50 Value

EC Number	IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
2.1.1.148	0.0083	-	pH not specified in the publication, temperature not specified in the publication	Mycobacterium tuberculosis	5-undecyloxymethyl-2'-deoxyuridine 5'-monophosphate

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Release 2023.1 (January 2023)