Covalent Protein Labeling by Enzymatic Phosphocholination

Angewandte Chemie, 2015, DOI: 10.1002/anie.201502618, 54, 1 – 5 published on 03.07.2015
Angewandte Chemie, online article
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.  

TU München
Helmholtz München
MPI of Neurobiology
MPI of Biochemistry