Structural highlights
FunctionA0A0M3KL45_KLEPN Glycine radical enzyme that catalyzes the cleavage of a C-N bond in choline, producing trimethylamine (TMA) and acetaldehyde.[HAMAP-Rule:MF_02058] Publication Abstract from PubMedCutC 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 gut microbiota, and its metabolite, trimethylamine oxide (TMAO), 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 the 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. Structure and function of CutC choline lyase from human microbiota bacterium Klebsiella pneumoniae.,Kalnins G, Kuka J, Grinberga S, Makrecka-Kuka M, Liepinsh E, Dambrova M, Tars K J Biol Chem. 2015 Jul 17. pii: jbc.M115.670471. PMID:26187464[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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