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Inhibitors of the Herbicidal Target IspD: Allosteric Site Binding
Author(s) -
Witschel Matthias C.,
Höffken H. Wolfgang,
Seet Michael,
Parra Liliana,
Mietzner Thomas,
Thater Frank,
Niggeweg Ricarda,
Röhl Franz,
Illarionov Boris,
Rohdich Felix,
Kaiser Johannes,
Fischer Markus,
Bacher Adelbert,
Diederich François
Publication year - 2011
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.201102281
Subject(s) - allosteric regulation , computational biology , chemistry , stereochemistry , computer science , enzyme , biochemistry , biology
The pick of the pockets : The first inhibitors for IspD, an enzyme from the non‐mevalonate pathway of isoprenoid biosynthesis, are described. High‐throughput‐screening revealed a hit with an IC 50 value of 140 n M . Co‐crystal structure analyses of the binding mode in the newly formed allosteric pocket (see structure, red ball: water O atom), lead to the synthesis of a set of 17 derivatives which were tested to optimize the herbicidal activity.