CutC Enzyme Crystal Structure and Inhibition Data for Gut Microbial Choline Metabolism

Research data on the gut microbial enzyme choline TMA-lyase (CutC) and its inhibition by betaine aldehyde. The dataset includes in vitro assay results and a crystal structure of the enzyme-inhibitor complex, produced by M.A. Funk at Harvard University. The workflow provides a framework for developing therapeutic inhibitors of a disease-linked metabolic pathway.

Use Cases

• Analyzing enzyme-inhibitor interactions based on the crystal structure of CutC with betaine aldehyde.
• Evaluating inhibitor efficacy based on in vitro assays of TMA production inhibition.
• Developing computational models for drug discovery based on the established inhibitor characterization framework.
• Comparing the activity of betaine aldehyde with the previously reported inhibitor 3,3-dimethylbutanol (DMB).

Strengths

• Includes a crystal structure, providing atomic-level detail of the enzyme-inhibitor complex.
• In vitro assay data validates the inhibitory effect of betaine aldehyde on TMA production.
• Research originates from Harvard University, suggesting a credible scientific foundation.

Limitations

• Row count and dataset size are unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

Harvard University

Collection Method

In vitro assays and X-ray crystallography, as described in the associated research.