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羊毛硫抗生素的翻译后修饰。

Post-translational modifications of lantibiotics.

作者信息

Kupke T, Götz F

机构信息

Mikrobielle Genetik, Universität Tübingen, Germany.

出版信息

Antonie Van Leeuwenhoek. 1996 Feb;69(2):139-50. doi: 10.1007/BF00399419.

Abstract

Several newly reported post-translational modification reactions are involved in lantibiotic biosynthesis. A short overview of the present knowledge on the post-translational modifications and on the enzymes involved in lantibiotic biosynthesis is given. The oxidative decarboxylation of the epidermin precursor peptide EpiA is described in detail. The FMN-containing oxidoreductase EpiD is involved in the formation of the C-terminal S-[(Z)-2-aminovinyl]-D-cysteine residue of epidermin: under reducing conditions the side chain of the C-terminal cysteine residue of EpiA is converted to an enethiol. EpiD has no absolute substrate specificity and can be used for modification of peptides having the C-terminal consensus motif [V/I/L/(M)/F/Y/W]-[A/S/V/T/C/(I/L)]-C.

摘要

几种新报道的翻译后修饰反应参与了羊毛硫抗生素的生物合成。本文简要概述了目前关于羊毛硫抗生素生物合成中翻译后修饰及相关酶的知识。详细描述了表皮菌素前体肽EpiA的氧化脱羧反应。含黄素单核苷酸(FMN)的氧化还原酶EpiD参与了表皮菌素C端S-[(Z)-2-氨基乙烯基]-D-半胱氨酸残基的形成:在还原条件下,EpiA C端半胱氨酸残基的侧链转化为烯硫醇。EpiD没有绝对的底物特异性,可用于修饰具有C端共有基序[V/I/L/(M)/F/Y/W]-[A/S/V/T/C/(I/L)]-C的肽。

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