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X-ray Structure of Human ACMSD with TES-1025

TES Pharma announces the publication of a Frontiers in Molecular Biosciences, section Structural Biology paper “ Structural basis of human dimeric α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD) inhibition with TES-1025” (doi.org/10.3389/fmolb.2022.834700) disclosing, by X-ray crystallography studies, the structure of human ACMSD in complex with TES-1025, the potent ACMSD inhibitor developed by TES Pharma.

The TES-1025 inhibitor has a Ki value of 0.85 ± 0.22 nM and binds in the catalytic site of the dimeric enzyme, interacting with the Zn2+ metal ion and with residues belonging to both chains of the dimer.

The results provide new structural information about the mechanism of inhibition exerted by this novel class of compounds on the ACMSD enzyme, an important therapeutic target for liver and kidney diseases.

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