Structural highlights
Publication Abstract from PubMedAziridine is a characteristically reactive molecule with increased bioactivity due to its strained ring structure. Here, we investigated the biosynthesis of 2-aminoisobutyric acid (AIB) in Penicillium , and successfully reconstituted the three-step biosynthesis from L-Val to AIB in vitro . This previously unknown aziridine formation pathway proceeded with the non-heme iron and a -ketoglutarate-dependent (Fe(II)/ alpha KG) oxygenase TqaL, followed by aziridine ring opening by the haloalkanoic acid dehalogenase (HAD)-type hydrolase TqaF, and subsequent oxidative decarboxylation by the NovR/CloR-like non-heme iron oxygenase TqaM. Furthermore, the X-ray crystal structure of the C-N bond forming Fe(II)/ alpha KG oxygenase TqaL was solved at 2.0 A resolution. This work presents the first molecular basis for aziridine biogenesis, thereby expanding the catalytic repertoire of the Fe(II)/ alpha KG oxygenases. We also report the unique aziridine ring opening by a HAD-type hydrolase and the remarkable oxidative decarboxylation by a non-heme iron oxygenase to produce AIB. Aziridine formation by a Fe(II)/alpha-ketoglutarate dependent oxygenase and 2-aminoisobutyrate biosynthesis in fungi.,Abe I, Bunno R, Awakawa T, Mori T Angew Chem Int Ed Engl. 2021 May 11. doi: 10.1002/anie.202104644. PMID:33973699[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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