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Structural Basis and Enzymatic Mechanism of the Biosynthesis of C 9 ‐ from C 10 ‐Monoterpenoid Indole Alkaloids
Author(s) -
Yang Liuqing,
Hill Marco,
Wang Meitian,
Panjikar Santosh,
Stöckigt Joachim
Publication year - 2009
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.200900150
Subject(s) - catalytic triad , biosynthesis , stereochemistry , enzyme , indole test , hydrolase , chemistry , serine , esterase , biochemistry
Cutting carbons : The three‐dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C 9 ‐ from C 10 ‐monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate‐specific serine esterase. It harbors the catalytic triad S87‐D216‐H244, and is a new member of the α/β‐fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.