Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase.

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Citation

Kanerva K, Makitie LT, Pelander A, Heiskala M, Andersson LC

Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase.

Biochem J. 2008 Jan 1;409(1):187-92.

PubMed ID
17900240 [ View in PubMed
]
Abstract

ODC (ornithine decarboxylase), the rate-limiting enzyme in polyamine biosynthesis, is regulated by specific inhibitors, AZs (antizymes), which in turn are inhibited by AZI (AZ inhibitor). We originally identified and cloned the cDNA for a novel human ODC-like protein called ODCp (ODC paralogue). Since ODCp was devoid of ODC catalytic activity, we proposed that ODCp is a novel form of AZI. ODCp has subsequently been suggested to function either as mammalian ADC (arginine decarboxylase) or as AZI in mice. Here, we report that human ODCp is a novel AZI (AZIN2). By using yeast two-hybrid screening and in vitro binding assay, we show that ODCp binds AZ1-3. Measurements of the ODC activity and ODC degradation assay reveal that ODCp inhibits AZ1 function as efficiently as AZI both in vitro and in vivo. We further demonstrate that the degradation of ODCp is ubiquitin-dependent and AZ1-independent similar to the degradation of AZI. We also show that human ODCp has no intrinsic ADC activity.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Ornithine decarboxylase antizyme 1P54368Details
Ornithine decarboxylaseP11926Details
Antizyme inhibitor 2Q96A70Details
Ornithine decarboxylase antizyme 2O95190Details
Ornithine decarboxylase antizyme 3Q9UMX2Details