Application | Comment | Organism |
---|---|---|
drug development | unexpected observation that NADP+ competes with both FAD and substrate for the binding site in ThyX and displaces both molecules from the active site, opens avenues for the design of tight-binding inhibitors of ThyX enzymes from a variety of organisms | Mycobacterium tuberculosis |
Cloned (Comment) | Organism |
---|---|
I65M/L175M double mutant expressed in Escherichia coli BL21 (DE3) pLysS strain as C-terminal His6-tagged protein | Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
I65M/L175M double mutant in the presence of FAD and BrdUMP, by the sitting-drop vapor-diffusion method, to 2.0 A resolution | Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
---|---|---|
I65M/L175M | produces active ThyX enzyme | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WG57 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WG57 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5,10-methylenetetrahydrofolate + BrdUMP + FADH2 | - |
Mycobacterium tuberculosis | ? | - |
? | |
5,10-methylenetetrahydrofolate + BrdUMP + FADH2 | - |
Mycobacterium tuberculosis H37Rv | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | - |
Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
flavin dependent thymidylate synthase | - |
Mycobacterium tuberculosis |
ThyX | - |
Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Mycobacterium tuberculosis | |
NADP+ | expulsion of the cofactor FAD by NADP+, no anticipated ThyX-FAD-BrdUMP-NADP+ quaternary complex, but a ThyX-NADP+ binary complex | Mycobacterium tuberculosis |