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Two‐fold Bioorthogonal Derivatization by Different Formylglycine‐Generating Enzymes |
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| Authors: | Tobias Krüger Dr. Stefanie Weiland Georg Falck Dr. Marcus Gerlach Mareile Boschanski Dr. Sarfaraz Alam Prof. Dr. Kristian M. Müller Prof. Dr. Thomas Dierks Prof. Dr. Norbert Sewald |
| Affiliation: | 1. Organische und Bioorganische Chemie, Fakult?t für Chemie, Universit?t Bielefeld, Bielefeld, Germany;2. Biochemie I, Fakult?t für Chemie, Universit?t Bielefeld, Bielefeld, Germany;3. Zellul?re und Molekulare Biotechnologie, Technische Fakult?t, Universit?t Bielefeld, Bielefeld, Germany |
| Abstract: | Formylglycine‐generating enzymes are of increasing interest in the field of bioconjugation chemistry. They catalyze the site‐specific oxidation of a cysteine residue to the aldehyde‐containing amino acid Cα‐formylglycine (FGly). This non‐canonical residue can be generated within any desired target protein and can subsequently be used for bioorthogonal conjugation reactions. The prototypic formylglycine‐generating enzyme (FGE) and the iron‐sulfur protein AtsB display slight variations in their recognition sequences. We designed specific tags in peptides and proteins that were selectively converted by the different enzymes. Combination of the different tag motifs within a single peptide or recombinant protein enabled the independent and consecutive introduction of two formylglycine residues and the generation of heterobifunctionalized protein conjugates. |
| Keywords: | bioconjugation enzyme catalysis formylglycine peptides radical-SAM enzymes |