Covalent Protein Labeling by Enzymatic Phosphocholination
2015 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 54, no 35, 10327-10330 p.Article in journal (Refereed) Published
We present a new protein labeling method based on the covalent enzymatic phosphocholination of a specific octapeptide amino acid sequence in intact proteins. The bacterial enzyme AnkX from Legionella pneumophila has been established to transfer functional phosphocholine moieties from synthetically produced CDP-choline derivatives to N-termini, C-termini, and internal loop regions in proteins of interest. Furthermore, the covalent modification can be hydrolytically removed by the action of the Legionella enzyme Lem3. Only a short peptide sequence (eight amino acids) is required for efficient protein labeling and a small linker group (PEG-phosphocholine) is introduced to attach the conjugated cargo.
Place, publisher, year, edition, pages
2015. Vol. 54, no 35, 10327-10330 p.
enzymes, nucleotides, phosphocholination, protein modifications
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:umu:diva-109454DOI: 10.1002/anie.201502618ISI: 000360216800050PubMedID: 26147231OAI: oai:DiVA.org:umu-109454DiVA: diva2:859709