Teufel Robin
ZBSA, Center for Biological Systems Analysis, University of Freiburg, Freiburg, Germany; Faculty of Biology, University of Freiburg, Freiburg, Germany.
Methods Enzymol. 2018;604:523-540. doi: 10.1016/bs.mie.2018.01.036. Epub 2018 Mar 16.
Flavoenzymes often function as oxygenases and have been extensively studied for many decades. Commonly, oxygenation reactions are mediated by a transient C4a-peroxyflavin formed from reaction of reduced flavin with O. EncM, however, employs a previously unrecognized flavin-oxygenating species, the flavin-N5-oxide, which is key to a complex oxidative Favorskii-type rearrangement and cyclization cascade in the biosynthesis of the bacterial polyketide antibiotic enterocin produced by the marine bacterium Streptomyces maritimus. Here, the methodology and key experiments are described that led to the discovery of this novel flavin redox species and granted insight into one of the most astounding single-enzyme-catalyzed reaction cascades in natural product biosynthesis.
黄素酶通常作为加氧酶发挥作用，并且已经被广泛研究了数十年。通常，氧化反应是由还原型黄素与氧气反应形成的瞬态C4a-过氧黄素介导的。然而，EncM利用了一种以前未被认识的黄素氧化物种，即黄素-N5-氧化物，它是海洋细菌马氏链霉菌产生的细菌聚酮类抗生素肠菌素生物合成中复杂氧化弗avorskii型重排和环化级联反应的关键。本文描述了导致发现这种新型黄素氧化还原物种的方法和关键实验，并深入了解了天然产物生物合成中最令人惊叹的单酶催化反应级联之一。
