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羊毛硫抗生素生物合成中涉及的独特肽修饰。

Unique peptide modifications involved in the biosynthesis of lantibiotics.

作者信息

Jack R W, Sahl H G

机构信息

Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Victoria, Australia.

出版信息

Trends Biotechnol. 1995 Jul;13(7):269-78. doi: 10.1016/S0167-7799(00)88962-3.

Abstract

The lantibiotics are a unique class of bacterium-derived peptide antibiotics, all of which contain the rare amino acid lanthionine, as well as a number of other nonprotein amino acids. Unlike most other peptide antibiotics, lantibiotics are produced on the ribosome as a prepeptide, and a series of post-translational modifications converts this precursor into the biologically active peptide. A complex set of gene products involved in lantibiotic biosynthesis have been identified, including the genes for specific amino acid modifications, as well as other ancillary biosynthetic functions. In the future, it should be possible to use some of these enzymes to engineer novel, non-protein amino acids into other proteins of biotechnological interest and importance.

摘要

羊毛硫抗生素是一类独特的源自细菌的肽抗生素,它们都含有稀有氨基酸羊毛硫氨酸以及一些其他非蛋白质氨基酸。与大多数其他肽抗生素不同,羊毛硫抗生素在核糖体上以前肽形式产生,一系列翻译后修饰将该前体转化为生物活性肽。已经鉴定出一组参与羊毛硫抗生素生物合成的复杂基因产物,包括特定氨基酸修饰的基因以及其他辅助生物合成功能。未来,应该有可能利用其中一些酶将新型非蛋白质氨基酸设计到其他具有生物技术意义和重要性的蛋白质中。

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