Exploring the mechanism of lipid transfer during biosynthesis of the acidic lipopeptide antibiotic CDA
Exploring the mechanism of lipid transfer during biosynthesis of the acidic lipopeptide antibiotic CDA
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DOI：
10.1016/j.febslet.2012.01.003
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发表时间：
2012-02-03
期刊：
影响因子：
3.5
通讯作者：
Marahiel, Mohamed A.
中科院分区：
文献类型：
--
作者：
Kraas, Femke I.;Giessen, Tobias W.;Marahiel, Mohamed A.
非核糖体合成的脂缩肽 CDA 属于酸性脂肽抗生素，其成员具有脂肪酸侧链，可强烈影响其抗菌活性。本研究阐明了 CDA 肽链中 N 末端丝氨酸的 N 酰化。该反应被称为脂肪引发，并且被证明是由 Cda-PSI N 末端的起始 C 结构域催化的。重组产生的 C 结构域与 2,3-环氧己酰基-S-ACP 特异性相互作用，并催化脂肪酸部分转移到 PCP 结合丝氨酸的氨基上，对供体和受体位点的载体蛋白结合底物具有高选择性。 (C) 2012 年欧洲生化学会联合会。由 Elsevier B.V. 出版。保留所有权利。
The non-ribosomally synthesized lipodepsipeptide CDA belongs to the group of acidic lipopeptide antibiotics, whose members feature a fatty acid side chain that strongly affects their antimicrobial activity. This study elucidates the N-acylation of the N-terminal serine in the CDA peptide chain. This reaction is referred to as lipoinitiation and is shown to be catalyzed by the dissected starter C domain found at the N-terminus of Cda-PSI. The recombinantly produced C domain specifically interacts with 2,3-epoxyhexanoyl-S-ACP and catalyzes the transfer of the fatty acid moiety onto the amino group of PCP-bound serine with high selectivity for both carrier protein bound substrates at the donor and acceptor site. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.