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Back Cover: Discovery of a Single Monooxygenase that Catalyzes Carbamate Formation and Ring Contraction in the Biosynthesis of the Legonmycins (Angew. Chem. Int. Ed. 43/2015)
Author(s) -
Huang Sheng,
Tabudravu Jioji,
Elsayed Somayah S.,
Travert Jeanne,
Peace Doe,
Tong Ming Him,
Kyeremeh Kwaku,
Kelly Sharon M.,
Trembleau Laurent,
Ebel Rainer,
Jaspars Marcel,
Yu Yi,
Deng Hai
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201506192
Subject(s) - pyrrolizidine , hydroxylation , decarboxylation , stereochemistry , chemistry , monooxygenase , biosynthesis , ring (chemistry) , carbamate , biocatalysis , enzyme , cytochrome p450 , biochemistry , organic chemistry , catalysis , reaction mechanism
The multifunctional Baeyer–Villiger enzyme LgnC catalyzes the transformation of indolizidines into pyrrolizidines by carbamate formation, hydrolysis, decarboxylation‐driven ring contraction, and hydroxylation. In their Communication on page 12697 ff., H. Deng, Y. Yu et al. show that these are the crucial steps for the biosynthesis of the legonmycins, new bacterial pyrrolizidine alkaloids named after their association with Legon, Ghana.