The AHAS enzyme's primary function is to start the process of biosynthesizing branched-chain amino acids , amino acids in which the aliphatic side-chain has a branch: valine, leucine, and isoleucine. These 3 are essential amino acids which are not synthesized in the human body but commonly found in plants, in particular Soybean. The action in the catalytic site for valine and leucine takes 2 pyruvate molecules CC(=O)C(=O)[O-] and converts these to acetolactate, CC(C(=O)O)OC(=O)C, through 2 CH3COCO2 -→ -O2CC(OH)(CH3)COCH3 + CO2 . The process for isoleucine uses 1 pyruvate and 1 2ketobutyrate, not 2 pyruvates. In addition to the use of cavity amino acids located in the catalytic site there are 3 cofactors to activate the AHAS enzyme: thiamine diphosphate (ThDP), 𝑀𝑔 +2 ions, and flavine-adenine dinucleotide (FAD). These resulting V,L,I produced aminos are eventually used by the plant for different purposes including reproduction via DNA synthesis; clearly, blocking an organism of its natural production of amino acids is going to cause survival problems. The AHAS active cavity amino acids used in the catalytic action are Glycine 511, Valine 485, Methionine 513, and Histidine 643, and others in the cavity placement alter binding, interaction, and transport. The numbering follows from the genomic sequence of Arabidopsis Thaliana (aka mouse-ear cress), Appendix 1.