| Autor: |
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., Zhai, Rui, Zhang, Wenjun |
| Zdroj: |
Nature Chemical Biology; December 2021, Vol. 17 Issue: 12 p1305-1313, 9p |
| Abstrakt: |
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 nitrite-utilizing, N-nitrosating enzyme (Tri17). This study paves the way for future mechanistic interrogation and biocatalytic application of enzymes for N–N bond formation. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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