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• W3216171611 endingPage "100007" @default.
• W3216171611 startingPage "100007" @default.
• W3216171611 abstract "In vitro characterization experiments revealed the formations of 3-(trans-2’-aminocyclopropyl)alanine ((3-Acp)Ala) and 3-(trans-2’-nitrocyclopropyl)alanine ((3-Ncp)Ala) are originated via two homologous proteins, BelK and HrmI, which regioselectively catalyze the Nε-oxygenation of l-lysine. The two enzymes belong to the emerging heme-oxygenase-like diiron oxidase and oxygenase (HDO) superfamily and the catalytic center of BelK is validated by homology modeling and site-directed mutations. Based on the in vitro characterization, the biosynthetic pathways of (3-Acp)Ala and (3-Ncp)Ala are proposed." @default.
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• W3216171611 date "2022-03-01" @default.
• W3216171611 modified "2023-10-14" @default.
• W3216171611 title "In vitro characterization of a nitro-forming oxygenase involved in 3-(trans-2’-aminocyclopropyl)alanine biosynthesis" @default.
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• W3216171611 doi "https://doi.org/10.1016/j.engmic.2021.100007" @default.
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