Phosphoethanolamine methyltransferases in phosphocholine biosynthesis: functions and potential for antiparasite therapy.

Phosphoethanolamine methyltransferases in phosphocholine biosynthesis: functions and potential for antiparasite therapy.
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磷酸胆碱生物合成中的磷酸乙醇胺甲基转移酶:抗寄生虫治疗的功能和潜力。

DOI:
10.1111/j.1574-6976.2011.00267.x
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发表时间:
2011-07
影响因子:
11.3
通讯作者:
Ben Mamoun C
Ben Mamoun C
中科院分区:
生物学1区
文献类型:
--
作者:
Bobenchik AM;Augagneur Y;Hao B;Hoch JC;Ben Mamoun C

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S-adenosyl-L-methionine-dependent methyltransferases represent a diverse group of enzymes that catalyze the transfer of a methyl group from a methyl donor S-adenosyl-L-methionine to nitrogen, oxygen, sulfur or carbon atoms of a large number of biologically active large and small molecules. These modifications play a major role in the regulation of various biological functions such as gene expression, signaling, nuclear division and metabolism. The three-step S-adenosyl-L-methionione-dependent methylation of phosphoethanolamine to form phosphocholine catalyzed by phosphoethanolamine N-methyltransferases has emerged as an important biochemical step in the synthesis of the major phospholipid, phosphatidylcholine, in some eukaryotes. Phosphoethanolamine N-methyltransferases have been identified in nematodes, plants, African clawed frogs, zebrafish, the Florida lancelet, proteobacteria and human malaria parasites. Data accumulated thus far suggest an important role for these enzymes in growth and development. This review summarizes published studies on the biochemical and genetic characterization of these enzymes, and discusses their evolution and their suitability as targets for the development of therapies against parasitic infections, as well as in bioengineering for the development of nutritional and stress-resistant plants.
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