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Synthesis and Evaluation of Acyl Protein Thioesterase 1 (APT1) Inhibitors
Author(s) -
Biel Markus,
Deck Patrick,
Giannis Athanassios,
Waldmann Herbert
Publication year - 2006
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200501128
Subject(s) - palmitoylation , thioesterase , myristoylation , prenylation , biochemistry , lipid anchored protein , enzyme , chemistry , function (biology) , signal transduction , microbiology and biotechnology , biology , cysteine , biosynthesis , phosphorylation , autophagy , apoptosis
Lipid‐modified proteins play decisive roles in important biological processes such as signal transduction, organisation of the cytoskeleton and vesicular transport. Lipidation of these proteins is essential for correct biological function. Among the modifications with lipids, prenylation and myristoylation are well understood. However, the machinery of palmitoylation is still under investigation. Recently, an enzyme, acyl protein thioesterase 1 (APT1), that may play a regulatory role in the palmitoylation cycle of H‐Ras and G‐protein α subunits, was purified. Motivated by this work, several inhibitors of APT1 were designed, synthesized and biologically evaluated leading to highly active compounds.