EC Number |
Application |
Reference |
---|
2.1.1.148 | 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 |
-, 681384 |
2.1.1.148 | medicine |
antibiotic target |
691759 |
2.1.1.148 | medicine |
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human |
637232, 637235 |
2.1.1.148 | medicine |
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45 |
637235 |
2.1.1.148 | medicine |
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low crossreactivity against mammalian thyA enzymes, EC 2.1.1.45 |
637235 |
2.1.1.148 | medicine |
the unique mechanism of FDTS makes it an attractive target for antibiotic drug development |
-, 658015 |
2.1.1.148 | medicine |
thymidylate synthase as a target for antitubercular drugs |
694812 |
2.1.1.148 | more |
autoregulates its own translation, RNA stem-loop structure acts as an inhibitory regulator of translation by preventing the binding of its Shine-Dalgarno-like sequence by positioning it in the stem region, addition of Thy1 into the in vitro translation system also inhibits translation |
678023 |
2.1.1.148 | more |
complements the Escherichia coli chi2913 strain that lacks its conventional TS activity, residues Lys165 and Arg168 play critical roles in ThyX activity, possibly by governing access to the carbon atom to be methylated of a totally buried substrate dUMP |
681375 |
2.1.1.148 | more |
residues His53, Glu190, Arg90, and Arg182 are essential for TS activity |
671555 |