Covalent Protein Labeling by Enzymatic Phosphocholination1. Issue 35 (3rd July 2015)

• Record Type: Journal Article
• Authors: Heller, Katharina; Ochtrop, Philipp; Albers, Michael F.; Zauner, Florian B.; Itzen, Aymelt; Hedberg, Christian
• Is Part Of: Angewandte Chemie international edition. Volume 54:Issue 35(2015)
• Page Start: 10327
• Page End: 10330
• Publication Date: 2015-07-03
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201502618
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>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.</p> </abstract>