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Defining Efficient Enzyme-Cofactor Pairs for Bioorthogonal Profiling of Protein Methylation

Proceedings of the National Academy of Sciences(2013)

Mem Sloan Kettering Canc Ctr

Cited 91|Views35
Abstract
Significance Many proteins undergo various posttranslational modifications for proper functions. One such modification is methylation carried out by enzyme–cofactor pairs of protein methyltransferases (PMTs) and S -adenosyl- L -methionine (SAM). Identification of methylated proteins is quite challenging because of the small size and chemical inertness of the methyl group. To address this challenge, we have synthesized SAM surrogates by replacing SAM’s methyl group with bulky, chemically active functionalities and demonstrated their utility as alternative cofactors of engineered PMTs for substrate labeling. Proteins modified with such chemical moieties are amenable to bioorthogonal reactions for subsequent enrichment and identification. An engineered enzyme–cofactor pair has been successfully used to reveal numerous methylated proteins.
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epigenetic,bump-hole,posttranslation,proteomics
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