Study of a New Compound for Inhibiting Enzymes
Author Information
Author(s): Wijeyesakere Sanjeeva J., Nasser Faik A., Kampf Jeff W., Aksinenko Alexey Y., Sokolov Vladimir B., Malygin Vladimir V., Makhaeva Galina F., Richardson Rudy J.
Primary Institution: University of Michigan
Hypothesis
Inhibition of serine hydrolases by FAP compounds occurs via scission of the P—C bond to organophosphorylate the active site serine.
Conclusion
The structure of diethyl-FAP revealed an elongated P—C bond that is expected to be labile, explaining its ability to inhibit serine hydrolases.
Supporting Evidence
- The compound's structure contains a P—C bond and two intermolecular hydrogen bonds, forming dimers.
- The elongated P—C bond in diethyl-FAP is similar to that in diisopentyl-FAP, suggesting similar reactivity.
- The study indicates that certain enzymes can break down stable P—C bonds, which could help in environmental cleanup.
Takeaway
Scientists created a new chemical compound that can stop certain enzymes from working, which could help in cleaning up harmful substances in the environment.
Methodology
The compound was synthesized by mixing diethylphosphite and the sulfonylimine of hexafluoroacetone, followed by recrystallization.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website