Author: Del Rio Flores, Antonio; Twigg, Frederick F.; Du, Yongle; Cai, Wenlong; Aguirre, Daniel Q.; Sato, Michio; Dror, Moriel J.; Narayanamoorthy, Maanasa; Geng, Jiaxin; Zill, Nicholas A.; Zhang, Wenjun
Title: Total Biosynthesis of Triacsin Featuring an N-hydroxytriazene Pharmacophore Cord-id: qf7d827j Document date: 2021_5_13
ID: qf7d827j
Snippet: 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
Document: 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.
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