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Molecular insights into the endoperoxide formation by Fe(II)/α-KG-dependent oxygenase NvfI
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Molecular insights into the endoperoxide formation by Fe(II)/α-KG-dependent oxygenase NvfI
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Journal Article
Molecular insights into the endoperoxide formation by Fe(II)/α-KG-dependent oxygenase NvfI
2021
Overview
Endoperoxide-containing natural products are a group of compounds with structurally unique cyclized peroxide moieties. Although numerous endoperoxide-containing compounds have been isolated, the biosynthesis of the endoperoxides remains unclear. NvfI from
Aspergillus novofumigatus
IBT 16806 is an endoperoxidase that catalyzes the formation of fumigatonoid A in the biosynthesis of novofumigatonin. Here, we describe our structural and functional analyses of NvfI. The structural elucidation and mutagenesis studies indicate that NvfI does not utilize a tyrosyl radical in the reaction, in contrast to other characterized endoperoxidases. Further, the crystallographic analysis reveals significant conformational changes of two loops upon substrate binding, which suggests a dynamic movement of active site during the catalytic cycle. As a result, NvfI installs three oxygen atoms onto a substrate in a single enzyme turnover. Based on these results, we propose a mechanism for the NvfI-catalyzed, unique endoperoxide formation reaction to produce fumigatonoid A.
Many endoperoxide-containing natural products have been isolated, but the biosynthesis of the endoperoxides remains unclear. Here, the authors report the structural and functional analysis of the NvfI endoperoxidase that catalyzes the formation of fumigatonoid A in the biosynthesis of novofumigatonin, and show that it does not employ tyrosyl radical in the reaction.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Ferrous Compounds - metabolism
/ Fungal Proteins - isolation & purification
/ Fungal Proteins - metabolism
/ Fungal Proteins - ultrastructure
/ Humanities and Social Sciences
/ Iron
/ Ketoglutaric Acids - metabolism
/ Oxygenases - isolation & purification
/ Peroxide
/ Protein Conformation, beta-Strand
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Recombinant Proteins - ultrastructure
/ Science
