Trimethyllysine: From Carnitine Biosynthesis to Epigenetics

Marijn N. Maas, Jordi C.J. Hintzen, Miriam R.B. Porzberg, Jasmin Mecinović*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

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Trimethyllysine is an important post-translationally modified amino acid with functions in the carnitine biosynthesis and regulation of key epigenetic processes. Protein lysine methyltransferases and demethylases dynamically control protein lysine methylation, with each state of methylation changing the biophysical properties of lysine and the subsequent effect on protein function, in particular histone proteins and their central role in epigenetics. Epigenetic reader domain proteins can distinguish between different lysine methylation states and initiate downstream cellular processes upon recognition. Dysregulation of protein methylation is linked to various diseases, including cancer, inflammation, and genetic disorders. In this review, we cover biomolecular studies on the role of trimethyllysine in carnitine biosynthesis, different enzymatic reactions involved in the synthesis and removal of trimethyllysine, trimethyllysine recognition by reader proteins, and the role of trimethyllysine on the nucleosome assembly.
Original languageEnglish
Article number9451
JournalInternational Journal of Molecular Sciences
Issue number24
Number of pages34
Publication statusPublished - Dec 2020


  • Carnitine
  • Epigenetics
  • Erasers
  • Methylation
  • Post‐translational modifications
  • Protein lysine demethylases
  • Protein lysine methyltransferases
  • Readers
  • Trimethyllysine
  • Writers


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