ArticlePloS one2011
Critical factors governing the difference in antizyme-binding affinities between human ornithine decarboxylase and antizyme inhibitor.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- Polyamines in Cancer: Mechanisms, Metabolic Targets, and Therapeutic Opportunities.Anti-cancer agents in medicinal chemistry · 2026Review
- AZIN1 level is increased in medulloblastoma and correlates with c-Myc activity and tumor phenotype.Journal of experimental & clinical cancer research : CR · 2025Article
- Protein degradation of antizyme depends on the N-terminal degrons.Protein science : a publication of the Protein Society · 2024Article
- Analyses of binding partners and functional domains for the developmentally essential protein Hmx3a/HMX3.Scientific reports · 2023Article
- Polyamines: Functions, Metabolism, and Role in Human Disease Management.Medical sciences (Basel, Switzerland) · 2021Review
- Role of Antizyme Inhibitor Proteins in Cancers and Beyond.OncoTargets and therapy · 2021Review
- Baicalein, 7,8-Dihydroxyflavone and Myricetin as Potent Inhibitors of Human Ornithine Decarboxylase.Nutrients · 2020Article
- Critical Factors in Human Antizymes that Determine the Differential Binding, Inhibition, and Degradation of Human Ornithine Decarboxylase.Biomolecules · 2019Article
- Developing a novel FRET assay, targeting the binding between Antizyme-AZIN.Scientific reports · 2019Article
- The antizyme family for regulating polyamines.The Journal of biological chemistry · 2018Review
- Antizyme Inhibitors in Polyamine Metabolism and Beyond: Physiopathological Implications.Medical sciences (Basel, Switzerland) · 2018Review
- Characterization of an androgen-responsive, ornithine decarboxylase-related protein in mouse kidney.Bioscience reports · 2017Article
- Antizyme inhibitor 1: a potential carcinogenic molecule.Cancer science · 2017Review
- Multifaceted interactions and regulation between antizyme and its interacting proteins cyclin D1, ornithine decarboxylase and antizyme inhibitor.Oncotarget · 2015Article
- Novel interaction of ornithine decarboxylase with sepiapterin reductase regulates neuroblastoma cell proliferation.Journal of molecular biology · 2014Article
- Article
- Structural and degradative aspects of ornithine decarboxylase antizyme inhibitor 2.FEBS open bio · 2014Article
- Determinants of the differential antizyme-binding affinity of ornithine decarboxylase.PloS one · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Both ornithine decarboxylase (ODC) and its regulatory protein, antizyme inhibitor (AZI), can bind with antizyme (AZ), but the latter has a higher AZ-binding affinity. The results of this study clearly identify the critical amino acid residues governing the difference in AZ-binding affinities between human ODC and AZI. Inhibition experiments using a series of ODC mutants suggested that residues 125 and 140 may be the key residues responsible for the differential AZ-binding affinities. The ODC_N125K/M140K double mutant demonstrated a significant inhibition by AZ, and the IC(50) value of this mutant was 0.08 µM, three-fold smaller than that of ODC_WT. Furthermore, the activity of the AZ-inhibited ODC_N125K/M140K enzyme was hardly rescued by AZI. The dissociation constant (K(d)) of the [ODC_N125K/M140K]-AZ heterodimer was approximately 0.02 µM, which is smaller than that of WT_ODC by approximately 10-fold and is very close to the K(d) value of AZI_WT, suggesting that ODC_N125K/M140K has an AZ-binding affinity higher than that of ODC_WT and similar to that of AZI. The efficiency of the AZI_K125N/K140M double mutant in the rescue of AZ-inhibited ODC enzyme activity was less than that of AZI_WT. The K(d) value of [AZI_K125N/K140M]-AZ was 0.18 µM, nine-fold larger than that of AZI_WT and close to the K(d) value of ODC_WT, suggesting that AZI_K125N/K140M has an AZ-binding affinity lower than that of AZI_WT and similar to that of ODC. These data support the hypothesis that the differences in residues 125 and 140 in ODC and AZI are responsible for the differential AZ-binding affinities.
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