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Acetohydroxyacid synthases: evolution, structure, and function

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Abstract

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.

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Acknowledgments

Funding was provided by grants from National Natural Science Foundation of China (NSFC31370131) and Six Talent Peaks Project of Jiangsu Province (2012-SWYY-008).

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Authors and Affiliations

  1. State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214000, China

    Yadi Liu, Yanyan Li & Xiaoyuan Wang

  2. School of Biotechnology, Jiangnan University, Wuxi, 214122, China

    Yadi Liu & Xiaoyuan Wang

  3. Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, 214122, China

    Xiaoyuan Wang

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  1. Yadi Liu
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Correspondence to Xiaoyuan Wang.

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Liu, Y., Li, Y. & Wang, X. Acetohydroxyacid synthases: evolution, structure, and function. Appl Microbiol Biotechnol 100, 8633–8649 (2016). https://doi.org/10.1007/s00253-016-7809-9

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