FOOD SCIENCE ›› 2019, Vol. 40 ›› Issue (11): 261-267.doi: 10.7506/spkx1002-6630-20180511-169

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Recent Progress in the Study of Homoserine O-Acyltransferase, the Key Enzyme in the Methionine Biosynthesis Pathway

LIU Shimeng, HAN Caijing, GAO Yunna, ZHAO Lan, LU Hongyan, MIN Weihong*   

  1. National Engineering Laboratory for Wheat and Corn Further Processing, College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China
  • Online:2019-06-15 Published:2019-06-28

Abstract: The first step in methionine synthesis is homoserine acylation catalyzed by homoserine acyltransferase to generate acylhomoserine. Homoserine O-acyltransferase, the key enzyme for methionine biosynthesis, is feedback inhibited or feedback repressed by the end products methionine and S-adenosylmethionine, and is easily inactivated at high temperatures, thus seriously affecting the flow of carbon toward methionine. In this context, studying and modifying homoserine O-acyltransferase are of great significance. However, there are few reports in the literature on studies and modification of homoserine O-acyltransferase. In the microbial metabolic pathways, inadequate carbon flow toward the methionine synthesis pathway can restrict microbial accumulation of methionine, and consequently hinder the industrial fermentation of methionine. In this paper, the role of homoserine O-acyltransferase in the methionine biosynthetic pathway is briefly described. Based on the structure catalytic mechanism of the enzyme as well as a review of recent studies on it, molecular modification strategies for feedback inhibition regulation and stability improvement are proposed.

Key words: methionine, homoserine O-acyltransferase, biosynthesis pathway, thermal stability

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