Cover Feature: An Unusual Fatty Acyl:Adenylate Ligase (FAAL)–Acyl Carrier Protein (ACP) Didomain in Ambruticin Biosynthesis (ChemBioChem 10/2018),ChemBioChem

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Cover Feature: An Unusual Fatty Acyl:Adenylate Ligase (FAAL)–Acyl Carrier Protein (ACP) Didomain in Ambruticin Biosynthesis (ChemBioChem 10/2018)
ChemBioChem ( IF 2.6 ) Pub Date : 2018-05-02 , DOI: 10.1002/cbic.201800207
Franziska Hemmerling _{1,

2} , Karen E. Lebe ₂ , Johannes Wunderlich ₁ , Frank Hahn _{1,

2}

Affiliation

The cover feature picture shows the adenylate‐forming‐acyl carrier protein (AFD‐ACP) didomain AmbG in action. This enzyme activates the product of the divinylcyclopropane‐forming rearrangement in ambruticin biosynthesis for further assembly‐line processing. Its biosynthetic role is indicated by its representation as a tamer in the ring. Bioinformatic analysis and in vitro experiments assigned the AFD of AmbG as a fatty acyl:adenylate ligase (FAAL) with an unusually broad substrate tolerance, thus suggesting that its natural substrate might indeed be a polyketide. More information can be found in the communication by F. Hahn et al. on page 1006 in Issue 10, 2018 (DOI: 10.1002/cbic.201800084).

中文翻译：

封面人物：Ambruticin生物合成中异常的脂肪酰基：腺苷酸连接酶（FAAL）-酰基载体蛋白（ACP）双结构域（ChemBioChem 10/2018）

封面特征图片显示了形成腺苷酸的酰基载体蛋白（AFD-ACP）双结构域AmbG。该酶激活了幕布素生物合成中二乙烯基环丙烷形成的重排产物，用于进一步的流水线处理。其生物合成作用由其在环中更温和的表示来表明。生物信息学分析和体外实验将AmbG的AFD指定为具有异常宽泛的底物耐受性的脂肪酰基：腺苷酸连接酶（FAAL），因此表明其天然底物的确可能是聚酮化合物。在F. Hahn等人的来文中可以找到更多信息。关于在第10期，2018页1006（：10.1002 / cbic.201800084 DOI）。

更新日期：2018-05-02

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