| Literature DB >> 30291781 |
Tobias Krüger1, Thomas Dierks2, Norbert Sewald1.
Abstract
Site-specific bioconjugation strategies offer many possibilities for directed protein modifications. Among the various enzyme-based conjugation protocols, formylglycine-generating enzymes allow to posttranslationally introduce the amino acid Cα-formylglycine (FGly) into recombinant proteins, starting from cysteine or serine residues within distinct consensus motifs. The aldehyde-bearing FGly-residue displays orthogonal reactivity to all other natural amino acids and can, therefore, be used for site-specific labeling reactions on protein scaffolds. In this review, the state of research on catalytic mechanisms and consensus motifs of different formylglycine-generating enzymes, as well as labeling strategies and applications of FGly-based bioconjugations are presented.Entities:
Keywords: AtsB; antibody-drug conjugates; bioorthogonal labeling; copper enzymes; enzyme immobilization; formylglycine; formylglycine-generating enzymes; radical-SAM proteins
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Year: 2019 PMID: 30291781 DOI: 10.1515/hsz-2018-0358
Source DB: PubMed Journal: Biol Chem ISSN: 1431-6730 Impact factor: 3.915