Amiri Moghaddam Jamshid, Guo Huijuan, Willing Karsten, Wichard Thomas, Beemelmanns Christine
Chemical Biology Leibniz Institute for Natural Product Research and Infection Biology e.V., Hans-Knöll-Institute, Beutenbergstraße 11a, 07745 Jena, Germany.
Bio Pilot Plant, Leibniz Institute for Natural Product Research and Infection Biology e.V., Hans-Knöll-Institute, Beutenbergstraße 11a, 07745 Jena, Germany.
Beilstein J Org Chem. 2022 Jun 22;18:722-731. doi: 10.3762/bjoc.18.72. eCollection 2022.
Aromatic prenylated metabolites have important biological roles and activities in all living organisms. Compared to their importance in all domains of life, we know relatively little about their substrate scopes and metabolic functions. Here, we describe a new UbiA-like prenyltransferase (Ptase) Ubi-297 encoded in a conserved operon of several bacterial taxa, including marine Flavobacteria and the genus . In silico analysis of Ubi-297 homologs indicated that members of this Ptase group are composed of several transmembrane α-helices and carry a conserved and distinct aspartic-rich Mg-binding domain. We heterologously produced UbiA-like Ptases from the bacterial genera , , and in . Investigation of their substrate scope uncovered the preferential farnesylation of quinoline derivatives, such as 8-hydroxyquinoline-2-carboxylic acid (8-HQA) and quinaldic acid. The results of this study provide new insights into the abundance and diversity of Ptases in marine Flavobacteria and beyond.
芳香族异戊烯化代谢产物在所有生物中都具有重要的生物学作用和活性。相较于它们在生命各个领域的重要性，我们对其底物范围和代谢功能的了解相对较少。在此，我们描述了一种新的类泛醌异戊烯基转移酶（Ptase）Ubi-297，它编码于几个细菌类群（包括海洋黄杆菌属和 属）的一个保守操纵子中。对Ubi-297同源物的计算机分析表明，该Ptase组的成员由几个跨膜α螺旋组成，并带有一个保守且独特的富含天冬氨酸的镁结合结构域。我们在 中异源表达了来自 属、 属和 属细菌的类泛醌异戊烯基转移酶。对它们底物范围的研究发现，喹啉衍生物（如8-羟基喹啉-2-羧酸（8-HQA）和喹哪啶酸）具有优先法尼基化作用。这项研究的结果为海洋黄杆菌属及其他生物中Ptase的丰度和多样性提供了新的见解。
