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Characterization and Crystal Structure of a Nonheme Diiron Monooxygenase Involved in Platensimycin and Platencin Biosynthesis.

著者 Dong LB , Liu YC , Cepeda AJ , Kalkreuter E , Deng MR , Rudolf JD , Chang C , Joachimiak A , Phillips GN , Shen B
J Am Chem Soc.2019 Jul 10 ; ():.
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Nonheme diiron monooxygenases make up a rapidly growing family of oxygenases that are rarely identified in secondary metabolism. Herein, we report the in vivo, in vitro, and structural characterizations of a nonheme diiron monooxygenase, PtmU3, that installs a C-5 -hydroxyl group in the unified biosynthesis of platensimycin and platencin, two highly functional-ized diterpenoids that act as potent and selective inhibitors of bacterial and mammalian fatty acid synthases. This hydroxyla-tion sets the stage for the subsequent A-ring cleavage step key to the unique diterpene-derived scaffolds of platensimycin and platencin. PtmU3 adopts an unprecedented triosephosphate isomerase (TIM)-barrel structural fold for this class of en-zymes and possesses a noncanonical diiron active site architecture with a saturated six-coordinate iron center lacking a μ-oxo bridge. This study reveals the first member of a previously unidentified superfamily of TIM-barrel fold enzymes for met-al-dependent dioxygen activation, with the majority predicted to act on CoA-linked substrates, thus expanding our knowledge of nature's repertoire of nonheme diiron monooxygenases and TIM-barrel fold enzymes.
PMID: 31291107 [PubMed - as supplied by publisher]
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