Author

R. Marmorstein

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Open access Aug 2026

Ligand-dependent interdomain rearrangements drive catalysis by acetyl-CoA synthetases.

Acetyl-coenzyme A synthetases convert ATP, acetate, and coenzyme A (CoA) into acetyl-CoA, a central metabolite that fuels lipid biosynthesis and regulates protein and RNA acetylation. ACS enzymes contain N- and C-terminal domains that coordinate a two-step ping-pong mechanism involving sequential adenylation and thioes...

Meng Li, Ming-Yang Zhou, R. Marmorstein · Structure · 0 citations

#protein folding Sep 2026

Tideglusib as a First-in-Class Chemical Probe for NatA: Identification, Mechanism, and Cellular Validation of an Allosteric, CoA-Dependent Inhibitor.

N-terminal acetyltransferase A (NatA) catalyzes 40-57% of eukaryotic Nα-acetylation, a co-translational modification critical for protein stability, localization, and function, yet no validated small-molecule probe of NatA has been reported. Here, we describe the discovery and characterization of tideglusib (YD3139), a...

Youchao Deng, Zhuojun Luo, Sarah M. Gardner et al. · ACS Chemical Biology · 0 citations