Formylglycine-generating enzymes for site-specific bioconjugation-Reference-Cited by-同舟云学术

Formylglycine-generating enzymes for site-specific bioconjugation

Published:2018-10-25 Issue:3 Volume:400 Page:289-297
ISSN:1437-4315
Container-title:Biological Chemistry
language:en
Short-container-title:

Author:

Krüger Tobias¹,Dierks Thomas²,Sewald Norbert¹

Affiliation:

1. Organic and Bioorganic Chemistry, Faculty of Chemistry , Bielefeld University , Universitätsstraße 25 , D-33615 Bielefeld , Germany

2. Biochemistry I, Faculty of Chemistry , Bielefeld University , Universitätsstraße 25 , D-33615 Bielefeld , Germany

Abstract

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.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Walter de Gruyter GmbH

Subject

Clinical Biochemistry,Molecular Biology,Biochemistry

Reference44 articles.

1. Agarwal, P., Kudirka, R., Albers, A.E., Barfield, R.M., de Hart, G.W., Drake, P.M., Jones, L.C., and Rabuka, D. (2013a). Hydrazino-Pictet-Spengler ligation as a biocompatible method for the generation of stable protein conjugates. Bioconjugate Chem. 24, 846–851.

2. Agarwal, P., van der Weijden, J., Sletten, E.M., Rabuka, D., and Bertozzi, C.R. (2013b). A Pictet-Spengler Ligation for protein chemical modification. Proc. Natl. Acad. Sci. USA 110, 46–51.

3. Appel, M.J. and Bertozzi, C.R. (2015). Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications. ACS Chem. Biol. 10, 72–84.

4. Benjdia, A., Dehò, G., Rabot, S., and Berteau, O. (2007). First evidences for a third sulfatase maturation system in prokaryotes from E. coli aslB and ydeM deletion mutants. FEBS Lett. 581, 1009–1014.

5. Berteau, O., Guillot, A., Benjdia, A., and Rabot, S. (2006). A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes. J. Biol. Chem. 281, 22464–22470.

Cited by 31 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Unleashing the Potential: Designing Antibody-Targeted Lipid Nanoparticles for Industrial Applications with CMC Considerations and Clinical Outlook;Molecular Pharmaceutics;2023-12-20

2. Detection, production, modification, and application of arylsulfatases;Biotechnology Advances;2023-10

3. Promiscuous Enzymes for Residue‐Specific Peptide and Protein Late‐Stage Functionalization;ChemBioChem;2023-07-19

4. Technology Advancement in Development of Antibody Drug Conjugates;PROG BIOCHEM BIOPHYS;2023

5. Antibody drug conjugates as targeted cancer therapy: past development, present challenges and future opportunities;Archives of Pharmacal Research;2023-04-18