1.1.1.3	additional information	no inhibition by [2-(1,1-dimethylethyl)-4-[[5-(1,1-dimethylethyl)-4-hydroxy-2-methylphenyl]thio]-5-methylphenoxy]-acetic acid and 4-amino-butyric acid 2-tert-butyl-4-(3-tert-butyl-4-hydroxy-phenylsulfanyl)-phenyl ester	2	
1.1.1.3	additional information	Thr does not inhibit homoserine dehydrogenase 1	2	
1.1.1.3	additional information	Lys, Met, and S-2-aminoethyl-L-cysteine do not affect HSDH activity at 1-5 mM	2	
1.1.1.3	additional information	enzyme is not inhibited by other aspartate-derived amino acids than threonine	2	
1.1.1.3	additional information	the natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine	2	
1.1.1.3	additional information	inhibitor docking study, overview	2	
1.1.1.3	additional information	molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Synergistic effects of HS1 and HS2 in combination with itraconazole against Paracoccidioides brasiliensis. Zinc1531037 and Zinc52986906 are not inhibitory	2	
1.1.1.3	additional information	molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 Molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Zinc1531037 and Zinc52986906 are not inhibitory	2	
1.1.1.3	additional information	L-homoserine inhibits the activity of aspartokinase encoded by metL	2	
1.1.1.3	additional information	L-homoserine oxidation of the Thermotoga maritima enzyme is almost impervious to inhibition by L-threonine, while L-threonine inhibits AK activity in a cooperative manner. The distinctive sequence of the regulatory domain in Thermotoga maritima AK-HseDH is likely responsible for the unique sensitivity to L-threonine. The quaternary structure of this enzyme is not affected by L-threonine	2