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Literature summary extracted from

  • Mathews, I.I.
    Flavin-dependent thymidylate synthase as a drug target for deadly microbes: mutational study and a strategy for inhibitor design (2013), J. Bioterror Biodef., Suppl 12, 004.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.148
-
 Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.148 mutant H53D, in complex with the methyl donor, CH2H4 folate. The substrate-binding loop can be stabilized in two conformations and this affects the binding of the molecules at the substrate binding site. The isoalloxazine (flavin) ring of FAD binds in a big pocket that tolerates large movements of the isoalloxazine ring. The isoalloxazine ring is able to rotate in the binding pocket and utilize same face of the ring to bind to substrate and cofactors Thermotoga maritima

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.148 H53D residue H53 is involved in folate binding. Crystal structures of the H53D-FAD and H53D-FAD-dUMP complexes Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.148 Thermotoga maritima Q9WYT0
-
-
2.1.1.148 Thermotoga maritima ATCC 43589 Q9WYT0
-
-

Synonyms

EC Number Synonyms Comment Organism
2.1.1.148 FDTS
-
 Thermotoga maritima