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Updated: Jul 20, 2026

11:31
Establishment of a High-throughput Setup for Screening Small Molecules That Modulate c-di-GMP Signaling in Pseudomonas aeruginosa
Published on: June 30, 2016
A new GNAT in bacterial signaling?
Structure (London, England : 1993)
|September 12, 2006
Summary
Novel acyl-amino acids, potential therapeutic agents from uncultured microbes, were identified. The N-acyl-amino acid synthase FeeM, bound to acyl-tyrosine, is a new member of the GCN5-related N-acyltransferase superfamily.
Area of Science:
- Biochemistry
- Microbiology
- Structural Biology
Background:
- Acyl-amino acids are compounds with potential therapeutic applications.
- These molecules are often produced by uncultured microorganisms, presenting a challenge for discovery.
- The search for novel therapeutic agents drives research into microbial metabolites.
Discussion:
- The N-acyl-amino acid synthase FeeM has been identified and characterized.
- FeeM binds to acyl-tyrosine, a specific type of acyl-amino acid.
- This enzyme's structure and function are relevant to understanding acyl-amino acid biosynthesis.
Key Insights:
- FeeM represents the most recent addition to the GCN5-related N-acyltransferase superfamily.
- The discovery provides structural insights into the mechanism of N-acyl-amino acid synthesis.
- This finding expands the known diversity of enzymes involved in acyl-amino acid metabolism.
Outlook:
- Further investigation of FeeM could reveal new therapeutic targets.
- Exploring uncultured microorganisms remains a promising avenue for novel drug discovery.
- Understanding the GCN5-related N-acyltransferase superfamily may lead to the development of new synthetic pathways.
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