Insights into the Desaturation of Cyclopeptin and its C3 Epimer Catalyzed by a non-Heme Iron Enzyme: Structural Characterization and Mechanism Elucidation
Journal
Angewandte Chemie - International Edition
Journal Volume
57
Journal Issue
7
Pages
1831-1835
Date Issued
2018
Author(s)
Liao H.-J.
Li J.
Huang J.-L.
Davidson M.
Kurnikov I.
Lin T.-S.
Lee J.L.
Kurnikova M.
Guo Y.
Chang W.-C.
Abstract
AsqJ, an iron(II)- and 2-oxoglutarate-dependent enzyme found in viridicatin-type alkaloid biosynthetic pathways, catalyzes sequential desaturation and epoxidation to produce cyclopenins. Crystal structures of AsqJ bound to cyclopeptin and its C3 epimer are reported. Meanwhile, a detailed mechanistic study was carried out to decipher the desaturation mechanism. These findings suggest that a pathway involving hydrogen atom abstraction at the C10 position of the substrate by a short-lived FeIV-oxo species and the subsequent formation of a carbocation or a hydroxylated intermediate is preferred during AsqJ-catalyzed desaturation.
SDGs
Publisher
Wiley-VCH Verlag
Type
journal article