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Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase

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A Structurally Diverse Compound Screening Library to Identify Substrates for Diamine, Polyamine, and Related

Hazel Leiva¹, Pamela L Caro De Silva^1,2, Ron Painter¹

¹San Francisco State University, Department of Chemistry and Biochemistry, San Francisco, California 94132, United States.

|December 23, 2024

Summary

Researchers investigated Gcn5-related N-acetyltransferase (GNAT) enzymes, including spermidine/spermine N-acetyltransferases (SSATs), to understand their substrate specificity. The study screened 17 GNAT enzymes against diverse amine-containing compounds, revealing varied acetylation activities and promiscuity.

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Area of Science:

Biochemistry
Enzymology
Molecular Biology

Background:

Spermidine/spermine N-acetyltransferases (SSATs) and other polyamine acetyltransferases (PAATs) are part of the Gcn5-related N-acetyltransferase (GNAT) superfamily.
Their substrate specificity and promiscuity toward various compounds, including polyamine-derived moieties, remain poorly understood.
Understanding these enzymes is crucial for elucidating the roles of acetylated small molecules in cellular processes.

Purpose of the Study:

To investigate the substrate specificity and promiscuity of 17 different GNAT enzymes.
To identify potential native substrates beyond simple polyamines for GNAT enzymes.
To gain fundamental insights into the acetylation capabilities of the GNAT superfamily.

Main Methods:

Screening of 17 GNAT enzymes against a diverse set of compounds containing primary amine moieties.
Compounds included diamines, triamines, and polyamines with variations in chain length and functional groups.
Assessing the acetylation activity of each enzyme toward the selected substrates.

Main Results:

Twelve out of the 17 screened GNAT enzymes exhibited acetylation activity toward at least one tested compound.
Some GNAT enzymes displayed high selectivity for a single substrate, while others showed promiscuity toward multiple compounds.
The study identified specific substrates that can be further explored to understand GNAT enzyme substrate scope.

Conclusions:

GNAT enzymes, including SSATs, exhibit a range of substrate specificities and promiscuities.
The findings highlight the potential for GNAT enzymes to acetylate a broader range of compounds than previously assumed.
Further research on identified substrates will clarify the biological significance of GNAT-mediated acetylation in cells.