ArticleThe Biochemical journal2021
Structural basis of binding and inhibition of ornithine decarboxylase by 1-amino-oxy-3-aminopropane.
Article in The Biochemical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- A direct fluorescence assay for quantitative analysis of ornithine decarboxylase activity and inhibitor screening.The Journal of biological chemistry · 2026Article
- Article
- Metabolic reprogramming in cancer: signaling pathways and therapeutic targets.Molecular cancer · 2026Review
- Multi-Temperature Crystallography of S-Adenosylmethionine Decarboxylase Observes Dynamic Loop Motions.Biomolecules · 2025Article
- Design, Synthesis, and Biological Activity of Novel Ornithine Decarboxylase (ODC) Inhibitors.Journal of medicinal chemistry · 2025Article
- Structure simulation-based comparison of active site variations in fungal ornithine decarboxylases.Communicative & integrative biology · 2025Article
- DMSO-tolerant ornithine decarboxylase (ODC) tandem assay optimised for high-throughput screening.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Structure and Enzymatic Activity of an Intellectual Disability-Associated Ornithine Decarboxylase Variant, G84R.ACS omega · 2022Article
- Biogenic Polyamines and Related Metabolites.Biomolecules · 2021Article
- Article
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
Abstract
Ornithine decarboxylase (ODC) is the rate-limiting enzyme for the synthesis of polyamines (PAs). PAs are oncometabolites that are required for proliferation, and pharmaceutical ODC inhibition is pursued for the treatment of hyperproliferative diseases, including cancer and infectious diseases. The most potent ODC inhibitor is 1-amino-oxy-3-aminopropane (APA). A previous crystal structure of an ODC-APA complex indicated that APA non-covalently binds ODC and its cofactor pyridoxal 5-phosphate (PLP) and functions by competing with the ODC substrate ornithine for binding to the catalytic site. We have revisited the mechanism of APA binding and ODC inhibition through a new crystal structure of APA-bound ODC, which we solved at 2.49 Å resolution. The structure unambiguously shows the presence of a covalent oxime between APA and PLP in the catalytic site, which we confirmed in solution by mass spectrometry. The stable oxime makes extensive interactions with ODC but cannot be catabolized, explaining APA's high potency in ODC inhibition. In addition, we solved an ODC/PLP complex structure with citrate bound at the substrate-binding pocket. These two structures provide new structural scaffolds for developing more efficient pharmaceutical ODC inhibitors.
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