Identification of Alp1U and Lom6 as epoxy hydrolases and implications for kinamycin and lomaiviticin biosynthesis

Bin Wang, Fang Guo, Jinwei Ren, Guomin Ai, Bertrand Aigle, Keqiang Fan () and Keqian Yang ()
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Bin Wang: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences
Fang Guo: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences
Jinwei Ren: State Key Laboratory of Mycology, Institute of Microbiology, Chinese Academy of Sciences
Guomin Ai: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences
Bertrand Aigle: Université de Lorraine, Dynamique des Génomes et Adaptation Microbienne, UMR 1128
Keqiang Fan: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences
Keqian Yang: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences

Nature Communications, 2015, vol. 6, issue 1, 1-5

Abstract: Abstract The naturally occurring diazobenzofluorenes, kinamycins, fluostatins and lomaiviticins, possess highly oxygenated A-rings, via which the last forms a dimeric pharmacophore. However, neither the A-ring transformation nor the dimerization mechanisms have been explored thus far. Here we propose a unified biosynthetic logic for the three types of antibiotics and verify one key reaction via detailed genetic and enzymatic experiments. Alp1U and Lom6 from the kinamycin and lomaiviticin biosynthesis, respectively, are shown to catalyse epoxy hydrolysis on a substrate that is obtained by chemical deacetylation of a kinamycin-pathway-derived intermediate. Thus, our study provides the first evidence for the existence of an epoxy intermediate in lomaiviticin biosynthesis. Furthermore, our results suggest that the dimerization in the lomaiviticin biosynthesis proceeds after dehydration of a product generated by Lom6.

Date: 2015
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DOI: 10.1038/ncomms8674

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