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Acetohydroxy acid synthase (AHAS) is a thiamin diphosphate (ThDP)-dependent enzyme involved in the biosynthesis of branched-chain amino acids (valine, leucine, and isoleucine) in plants, bacteria, and fungi. This makes AHAS an attractive target for herbicides and bactericides, which act by interrupting the catalytic cycle and preventing the synthesis of acetolactate and 2-keto-hydroxybutyrate intermediates, in the biosynthetic pathway toward the synthesis of branched amino acids, causing the death of the organism. Several articles on the catalytic cycle of AHAS have been published in the literature; however, there are certain aspects, which continue being controversial or unknown. This lack of information at the molecular level makes difficult the rational development of novel herbicides and bactericides, which act inhibiting this enzyme. In this chapter, we review the results from our group for the different stages of the catalytic cycle of AHAS, using both quantum chemical cluster and Quantum Mechanics/Molecular Mechanics approaches.

A Computational Chemistry Approach for the Catalytic Cycle of AHAS