9HT9 image
Deposition Date 2024-12-19
Release Date 2026-01-14
Last Version Date 2026-02-25
Entry Detail
PDB ID:
9HT9
Keywords:
Title:
CutC in complex with inhibitor1
Biological Source:
Source Organism(s):
Expression System(s):
Method Details:
Experimental Method:
Resolution:
1.84 Å
R-Value Free:
0.21
R-Value Work:
0.18
R-Value Observed:
0.18
Space Group:
P 1
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Choline trimethylamine-lyase
Gene (Uniprot):cutC
Chain IDs:A, B, C, D
Chain Length:800
Number of Molecules:4
Biological Source:Oleidesulfovibrio alaskensis
Ligand Molecules
Primary Citation
Discovery of a Highly Potent and Selective Small-Molecule Inhibitor of In Vivo Anaerobic Choline Metabolism by Human Gut Bacteria.
J.Med.Chem. 69 2115 2129 (2026)
PMID: 41614677 DOI: 10.1021/acs.jmedchem.5c01451

Abstact

Trimethylamine (TMA) Lyase is an enzyme expressed in human gut bacteria that plays a pivotal role in the formation of trimethylamine oxide (TMAO), a metabolite implicated in the development of heart failure. Here, we describe a strategy to design covalent inhibitors targeting the active site thiyl radical involved in the catalytic cycle of the enzyme under anaerobic conditions. This strategy led to the discovery of 7, a previously unreported highly potent and selective inhibitor of TMA Lyase. When dosed orally to rats, 7 shows a significant reduction of circulating TMAO levels and, importantly, demonstrates inhibition of TMAO generated from a human microbiome when profiled in a human fecal mouse transplant model.

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Primary Citation of related structures
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