In greenhouse studies, the calculated I50 (herbicide application resulting in 50% inhibition of shoot regrowth) in tall fescue was approximately 0.004 kg/ha for both sethoxydim and haloxyfop. In red fescue, the I50 for sethoxydim and haloxyfop was 9.4 kg/ha and 0.04 kg/ha, respectively. As measured in crude cell extracts of tall fescue, incorporation of 14C-acetyl-coenzyme A into fatty acids was inhibited 62 and 71% by 10 μM sethoxydim and 10 μM haloxyfop, respectively. In red fescue, 10 μM haloxyfop inhibited 14C-acetyl-CoA incorporation into fatty acids by 29%, whereas 10 μM sethoxydim had no effect. The I50 for inhibition of acetyl-coenzyme A carboxylase activity in tall fescue with sethoxydim and haloxyfop was 6.9 and 5.8 μM, respectively. In red fescue the I50 for haloxyfop was 118 μM. Sethoxydim concentrations as high as 1 mM had little effect on acetyl-coenzyme A carboxylase activity in red fescue. These results suggest that acetyl-coenzyme A carboxylase is a sensitive site of action for sethoxydim and haloxyfop in tall fescue, and that tolerance to these herbicides in red fescue is due to the presence of a more tolerant form of the enzyme.

The crystal structure of the Escherichia coli enoyl reductase-NAD+-triclosan complex has been determined at 2.5 Å resolution. The Ile192–Ser198 loop is either disordered or in an open conformation in the previously reported structures of the enzyme. This loop adopts a closed conformation in our structure, forming van der Waals interactions with the inhibitor and hydrogen bonds with the bound NAD+ cofactor. The opening and closing of this flipping loop is likely an important factor in substrate or ligand recognition. The closed conformation of the loop appears to be a critical feature for the enhanced binding potency of triclosan, and a key component in future structure-based inhibitor design.