. Author manuscript; available in PMC: 2008 Nov 30.

Published in final edited form as: J Mol Biol. 2007 Oct 22;374(3):764–776. doi: 10.1016/j.jmb.2007.09.062

Table 1.

Structures of natural substrates of bacterial Tgt and the inhibitor 2-butyl-1H-imidazole-4,5-dicarboxylic acid hydrazide (BIH). In the line “conformation” the functional group of the Leu²³¹/Ala²³² peptide bond exposed to the binding pocket is given.

conformation	carbonyl Leu²³¹H-bonded Glu²³⁵ (deprotonated)	amide Ala²³²H-bonded Glu²³⁵ (protonated)	amide Ala²³² stacking Glu²³⁵ (protonated)
natural substrates	K_M: 0.7 μM	K_M: 1.2 μM	K_M: 0.9 M
inhibitor	K_ic: 62 μM