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Chemical‐Biological Exploration of the Limits of the Ras De‐ and Repalmitoylating Machinery
Author(s) -
Görmer Kristina,
Bürger Marco,
Kruijtzer John A. W.,
Vetter Ingrid,
Vartak Nachiket,
Brunsveld Lucas,
Bastiaens Philippe I. H.,
Liskamp Rob M. J.,
Triola Gemma,
Waldmann Herbert
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200078
Subject(s) - peptoid , substrate (aquarium) , computational biology , amino acid , computer science , sequence (biology) , chemistry , substrate specificity , biochemistry , stereochemistry , biology , peptide , enzyme , ecology
A dynamic de‐/repalmitoylation cycle determines localization and activity of H‐ and N‐Ras. This combined cellular de‐ and repalmitoylation machinery has been shown to be substrate tolerant—it accepts variation of amino acid sequence, structure and configuration. Here, semisynthetic Ras‐proteins in which the C‐terminal amino acids are replaced by peptoid residues are used to reveal the first limitations of substrate recognition by the de‐ and repalmitoylating machinery.