Different roles for the acyl chain and the amine leaving group in the substrate selectivity of N-Acylethanolamine acid amidase
Laboratory studyOther animals
- Design
- Laboratory study
- Subjects
- Enzyme assays and molecular dynamics simulations; no animals or people
- Dose used in the study
- Not applicable; substrates were tested against the NAAA enzyme in vitro
- Duration
- Not stated in the abstract
- What was measured
- Catalytic efficiency of NAAA, the enzyme that breaks down palmitoylethanolamide, against fatty acid ethanolamides with different acyl chain lengths and polar head groups, matched to modelled enzyme-substrate stability.
What the authors reported
Catalytic efficiency depended strictly on fatty acyl chain length in both saturated and monounsaturated substrates, while the enzyme tolerated a wider range of polar head changes. This matched the stability of enzyme-substrate complexes in simulations.
Limits of this study
An enzyme and computer-modelling study; it cannot show any effect in people or animals treated in practice. Two authors are inventors on patents covering NAAA inhibitors.
Source
PubMed 34256657 · doi:10.1080/14756366.2021.1912035
Entry checked against the abstract on PubMed on 2026-09-22. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.