Organische und Bioorganische Chemie, Fakultät für Chemie, Universität Bielefeld, Universitätsstraße 25, 33615, Bielefeld, Germany.
Biochemie I, Fakultät für Chemie, Universität Bielefeld, Universitätsstraße 25, 33615, Bielefeld, Germany.
Angew Chem Int Ed Engl. 2018 Jun 11;57(24):7245-7249. doi: 10.1002/anie.201803183. Epub 2018 May 9.
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 C -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.
甲酰甘氨酸生成酶在生物偶联化学领域越来越受到关注。它们催化半胱氨酸残基的位点特异性氧化生成含醛基的氨基酸 C -甲酰甘氨酸（FGly）。这种非典型的残基可以在任何所需的靶蛋白中产生，随后可用于生物正交的缀合反应。典型的甲酰甘氨酸生成酶（FGE）和铁硫蛋白 AtsB 在其识别序列上略有差异。我们在肽和蛋白质中设计了特定的标签，这些标签可以被不同的酶选择性地转化。在单个肽或重组蛋白中组合不同的标签基序，可以独立且连续地引入两个甲酰甘氨酸残基，并生成杂双功能化的蛋白质缀合物。
