Research ExplorerPublicationsCovalent Protein Labeling by Enzymatic Phosphocholination

Covalent Protein Labeling by Enzymatic Phosphocholination

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Covalent Protein Labeling by Enzymatic Phosphocholination. / Heller, Katharina; Ochtrop, Philipp; Albers, Michael F; Zauner, Florian B; Itzen, Aymelt; Hedberg, Christian.

In: ANGEW CHEM INT EDIT, Vol. 54, No. 35, 24.08.2015, p. 10327-30.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Heller, K, Ochtrop, P, Albers, MF, Zauner, FB, Itzen, A & Hedberg, C 2015, 'Covalent Protein Labeling by Enzymatic Phosphocholination', ANGEW CHEM INT EDIT, vol. 54, no. 35, pp. 10327-30. https://doi.org/10.1002/anie.201502618

APA

Heller, K., Ochtrop, P., Albers, M. F., Zauner, F. B., Itzen, A., & Hedberg, C. (2015). Covalent Protein Labeling by Enzymatic Phosphocholination. ANGEW CHEM INT EDIT, 54(35), 10327-30. https://doi.org/10.1002/anie.201502618

Vancouver

Heller K, Ochtrop P, Albers MF, Zauner FB, Itzen A, Hedberg C. Covalent Protein Labeling by Enzymatic Phosphocholination. ANGEW CHEM INT EDIT. 2015 Aug 24;54(35):10327-30. https://doi.org/10.1002/anie.201502618

Bibtex

@article{d1b3dd9dc13c40dfac1f7416c131b2d0,
title = "Covalent Protein Labeling by Enzymatic Phosphocholination",
abstract = "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. ",
keywords = "Ankyrin Repeat, Bacterial Proteins, Catalytic Domain, Hydrolases, Legionella pneumophila, Models, Molecular, Phosphorylcholine, Protein Processing, Post-Translational, Journal Article, Research Support, Non-U.S. Gov't",
author = "Katharina Heller and Philipp Ochtrop and Albers, {Michael F} and Zauner, {Florian B} and Aymelt Itzen and Christian Hedberg",
note = "{\textcopyright} 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",
year = "2015",
month = aug,
day = "24",
doi = "10.1002/anie.201502618",
language = "English",
volume = "54",
pages = "10327--30",
journal = "ANGEW CHEM INT EDIT",
issn = "1433-7851",
publisher = "John Wiley and Sons Ltd",
number = "35",

}

RIS

TY - JOUR

T1 - Covalent Protein Labeling by Enzymatic Phosphocholination

AU - Heller, Katharina

AU - Ochtrop, Philipp

AU - Albers, Michael F

AU - Zauner, Florian B

AU - Itzen, Aymelt

AU - Hedberg, Christian

N1 - © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

PY - 2015/8/24

Y1 - 2015/8/24

N2 - 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.

AB - 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.

KW - Ankyrin Repeat

KW - Bacterial Proteins

KW - Catalytic Domain

KW - Hydrolases

KW - Legionella pneumophila

KW - Models, Molecular

KW - Phosphorylcholine

KW - Protein Processing, Post-Translational

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1002/anie.201502618

DO - 10.1002/anie.201502618

M3 - SCORING: Journal article

C2 - 26147231

VL - 54

SP - 10327

EP - 10330

JO - ANGEW CHEM INT EDIT

JF - ANGEW CHEM INT EDIT

SN - 1433-7851

IS - 35

ER -