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Expanding cofactor repertoire of protein lysine methyltransferase for substrate labeling.

Protein lysine methyltransferases (PKMTs) play crucial roles in normal physiology and disease processes. Profiling PKMT targets is an important but challenging task. With cancer-relevant G9a as a target, we have demonstrated success in developing S-adenosyl-L-methionine (SAM) analogues, particularly (E)-hex-2-en-5-ynyl SAM (Hey-SAM), as cofactors for engineered G9a. Hey-SAM analogue in combination with G9a Y1154A mutant modifies the same set of substrates as their native counterparts with remarkable efficiency. (E)-Hex-2-en-5-ynylated substrates undergo smooth click reaction with an azide-based probe. This approach is thus suitable for substrate characterization of G9a and expected to further serve as a starting point to evolve other PKMTs to utilize a similar set of cofactors.

Pubmed ID: 21495674


  • Islam K
  • Zheng W
  • Yu H
  • Deng H
  • Luo M


ACS chemical biology

Publication Data

July 15, 2011

Associated Grants

  • Agency: NIH HHS, Id: 1-DP2-OD007335-01
  • Agency: NIGMS NIH HHS, Id: 1R01GM096056-01
  • Agency: NIH HHS, Id: DP2 OD007335
  • Agency: NIH HHS, Id: DP2 OD007335-01
  • Agency: NIGMS NIH HHS, Id: R01 GM096056
  • Agency: NIGMS NIH HHS, Id: R01 GM096056-01
  • Agency: NIGMS NIH HHS, Id: R01 GM096056-02

Mesh Terms

  • Coenzymes
  • Histocompatibility Antigens
  • Histone-Lysine N-Methyltransferase
  • Humans
  • Mutation
  • S-Adenosylmethionine