ArticleAmino acids2026
Revisiting the antizyme 1 - ODC interaction reveals low-nanomolar affinity.
Article in Amino acids, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Ornithine decarboxylase (ODC) catalyzes the rate-limiting step in polyamine biosynthesis and is one of the shortest-lived mammalian proteins. Its activity and proteasomal degradation are controlled by antizyme (AZ), which disrupts the active ODC homodimer and exposes proteasome-interacting surfaces. Disturbance of the polyamine biosynthesis pathway and their overproduction is associated with multiple diseases, including cancers. We employed activity assays and direct interaction analysis methods to quantify ODC-AZ interaction. Fluorometric activity assay, surface plasmon resonance, microscale thermophoresis and spectral shift assays allowed consistent determination of AZ-ODC binding with previously unavailable sensitivity. Contrary to former studies of this interaction, we show that binding of AZ to ODC occurs with a single-digit nanomolar affinity. Collectively, our orthogonal assays converge on a low-nanomolar interaction (apparent K
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