Rational Engineering of the Nonheme Iron- and 2‑Oxoglutarate-Dependent Oxygenase SptF

The Fe- and 2-oxoglutarate-dependent oxygenase SptF is a promising powerful biocatalys with unusual catalytic versatility and promiscuity. The site-specific random substitution of N150, I63, and N65, which are involved in substrate interactions, generated three compounds that were not produced by th...

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Veröffentlicht in:Organic letters 2022-03, Vol.24 (8), p.1737-1741
Hauptverfasser: Mori, Takahiro, Yu, Ziheng, Tao, Hui, Abe, Ikuro
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container_issue 8
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container_title Organic letters
container_volume 24
creator Mori, Takahiro
Yu, Ziheng
Tao, Hui
Abe, Ikuro
description The Fe- and 2-oxoglutarate-dependent oxygenase SptF is a promising powerful biocatalys with unusual catalytic versatility and promiscuity. The site-specific random substitution of N150, I63, and N65, which are involved in substrate interactions, generated three compounds that were not produced by the SptF wild type. The substrate binding mode was dramatically altered by the introduction of only one or two substitutions. These results provide insights into the engineering of Fe- and 2-oxoglutarate-dependent oxygenases for chemoenzymatic syntheses of bioactive compounds.
doi_str_mv 10.1021/acs.orglett.2c00409
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subjects Iron - chemistry
Iron - metabolism
Ketoglutaric Acids - chemistry
Ketoglutaric Acids - metabolism
Molecular Structure
Oxygenases - chemistry
Oxygenases - metabolism
Protein Engineering
Substrate Specificity
title Rational Engineering of the Nonheme Iron- and 2‑Oxoglutarate-Dependent Oxygenase SptF
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