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	additional information	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	additional information	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	additional information	residues His53, Glu190, Arg90, and Arg182 are essential for TS activity	671555