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Acetohydroxyacid synthases: evolution, structure, and function
- Liu, Yadi, Li, Yanyan, Wang, Xiaoyuan
- Applied microbiology and biotechnology 2016 v.100 no.20 pp. 8633-8649
- Archaea, acetolactate synthase, animals, anti-infective agents, bacteria, biochemical pathways, evolution, fungi, herbicides, plants (botany), pyruvic acid, thiamin, valine
- Acetohydroxyacid synthase, a thiamine diphosphate-dependent enzyme, can condense either two pyruvate molecules to form acetolactate for synthesizing L-valine and L-leucine or pyruvate with 2-ketobutyrate to form acetohydroxybutyrate for synthesizing L-isoleucine. Because the key reaction catalyzed by acetohydroxyacid synthase in the biosynthetic pathways of branched-chain amino acids exists in plants, fungi, archaea, and bacteria, but not in animals, acetohydroxyacid synthase becomes a potential target for developing novel herbicides and antimicrobial compounds. In this article, the evolution, structure, and catalytic mechanism of acetohydroxyacid synthase are summarized.