Covalent Protein Labeling by Enzymatic Phosphocholination
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.
Heller, Katharina,Ochtrop, Philipp,Albers, Michael F.,Zauner, Florian B.,Itzen, Aymelt,Hedberg, Christian
supporting information
p. 10327 - 10330
(2015/09/01)
SYNTHESIS OF CYTIDINE DIPHOSPHATE-D-QUINOVOSE
The title molecule, cytidine-D-quinovose (CDP-6-deoxy-D-glucose) 1, was synthesized by two different methods from the key intermediate quinovose-1-phosphate 7 which was prepared from glucose.
Liu, Li-da,Liu, Hung-wen
p. 35 - 38
(2007/10/02)
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