Structure and function of CutC choline lyase from human microbiota bacterium Klebsiella pneumoniae

Gints Kalnins, Janis Kuka, Solveiga Grinberga, Marina Makrecka-Kuka, Edgars Liepinsh, Maija Dambrova, Kaspars Tars

Research output: Contribution to journalArticlepeer-review

72 Citations (Scopus)
61 Downloads (Pure)


CutC choline trimethylamine-lyase is an anaerobic bacterial glycyl radical enzyme (GRE) that cleaves choline to produce trimethylamine (TMA) and acetaldehyde. In humans, TMA is produced exclusively by the intestinal microbiota, and its metabolite, trimethylamine oxide, has been associated with a higher risk of cardiovascular diseases. Therefore, information about the three-dimensional structures of TMA-producing enzymes is important for microbiota-targeted drug discovery. We have cloned, expressed, and purified the CutC GRE and the activating enzyme CutD from Klebsiella pneumoniae, a representative of the human microbiota. We have determined the first crystal structures of both the choline-bound and choline-free forms of CutC and have discovered that binding of choline at the ligand-binding site triggers conformational changes in the enzyme structure, a feature that has not been observed for any other characterized GRE.

Original languageEnglish
Pages (from-to)21732-21740
Number of pages9
JournalJournal of Biological Chemistry
Issue number35
Publication statusPublished - 28 Aug 2015
Externally publishedYes

Field of Science*

  • 1.6 Biological sciences
  • 3.1 Basic medicine

Publication Type*

  • 1.1. Scientific article indexed in Web of Science and/or Scopus database


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