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- W3160154851 abstract "Abstract Triacsins are an intriguing class of specialized metabolites possessing a conserved N -hydroxytriazene moiety not found in any other known natural products. Triacsins are notable as potent acyl-CoA synthetase inhibitors in lipid metabolism, yet their biosynthesis has remained elusive. Through extensive mutagenesis and biochemical studies, we here report all enzymes required to construct and install the N -hydroxytriazene pharmacophore of triacsins. Two distinct ATP-dependent enzymes were revealed to catalyze the two consecutive N-N bond formation reactions, including a glycine-utilizing hydrazine-forming enzyme, Tri28, and a nitrous acid-utilizing N -nitrosating enzyme, Tri17. This study paves the way for future mechanistic interrogation and biocatalytic application of enzymes for N-N bond formation." @default.
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- W3160154851 date "2021-05-13" @default.
- W3160154851 modified "2023-10-18" @default.
- W3160154851 title "Total Biosynthesis of Triacsin Featuring an N-hydroxytriazene Pharmacophore" @default.
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- W3160154851 doi "https://doi.org/10.1101/2021.05.12.443849" @default.
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