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Involvement of the Baeyer–Villiger Monooxygenase IfnQ in the Biosynthesis of Isofuranonaphthoquinone Scaffold of JBIR‐76 and ‐77
Author(s) -
Katsuyama Yohei,
Sone Kaoru,
Satou Ryutaro,
Izumikawa Miho,
Takagi Motoki,
Fujie Manabu,
Satoh Noriyuki,
Shinya Kazuo,
Ohnishi Yasuo
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600095
Subject(s) - monooxygenase , biosynthesis , scaffold , chemistry , biochemistry , enzyme , cytochrome p450 , medicine , biomedical engineering
JBIR‐76 and ‐77 are isofuranonaphthoquinones (IFNQs) isolated from Streptomyces sp. RI‐77. Draft genome sequencing and gene disruption analysis of Streptomyces sp. RI‐77 showed that a type II polyketide synthase (PKS) gene cluster ( ifn cluster) was responsible for the biosynthesis of JBIR‐76 and ‐77. It was envisaged that an octaketide intermediate (C 16 ) could be synthesized by the minimal PKS (IfnANO) and that formation of the IFNQ scaffold (C 13 ) would therefore require a C−C bond cleavage reaction. An ifnQ disruptant accumulated some shunt products (C 15 ), which were presumably produced by spontaneous cyclization of the decarboxylated octaketide intermediate. Recombinant IfnQ catalyzed the Baeyer–Villiger oxidation of 1‐(2‐naphthyl)acetone, an analogue of the bicyclic octaketide intermediate. Based on these results, we propose a pathway for the biosynthesis of JBIR‐76 and ‐77, involving IfnQ‐catalyzed C−C bond cleavage as a key step in the formation of the IFNQ scaffold.