These authors contributed equally to this work.
A Chemical Probe for Lysine Malonylation†
Article first published online: 26 MAR 2013
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 52, Issue 18, pages 4883–4886, April 26, 2013
How to Cite
Bao, X., Zhao, Q., Yang, T., Fung, Y. M. E. and Li, X. D. (2013), A Chemical Probe for Lysine Malonylation . Angew. Chem. Int. Ed., 52: 4883–4886. doi: 10.1002/anie.201300252
We thank Prof. Chi-Ming Che for generous support on the mass spectrometer, Prof. Dan Yang for advice and support, Prof. Quan Hao for useful discussions, and Di Hu for technical assistance. X.D.L. acknowledges a seed fund from The University of Hong Kong (201111159240) and Hung Hing Ying Physical Science Research Fund (20373739). Y.M.E.F. thanks the Small Project Funding from The University of Hong Kong (201109176193) and the Special Equipment Grant from the University Grants Committee of the Hong Kong Special Administrative Region, China (Project Code: SEG_HKU02).
- Issue published online: 21 APR 2013
- Article first published online: 26 MAR 2013
- Manuscript Revised: 4 FEB 2013
- Manuscript Received: 11 JAN 2013
- University of Hong Kong. Grant Number: 201111159240
- Hung Hing Ying Physical Science Research Fund. Grant Numbers: 20373739, 201109176193
- University Grants Committee of the Hong Kong Special Administrative Region. Grant Number: SEG_HKU02
- click chemistry;
- lysine malonylation;
- metabolic labeling;
- posttranslational modifications;
- protein modifications
Tag! You′re it! MalAM-yne is a chemical reporter for malonylation of lysines within proteins (see scheme), a newly identified posttranslational modification. MalAM-yne is cell-permeable and metabolically incorporated into proteins in living cells. Subsequent bioorthogonal tag conjugation allows the fluorescent visualization of cellular malonylation and profiling of malonylated proteins.