Ornithine decarboxylase (ODC) is a key enzyme in the biosynthesis of polyamines， organic cations that are implicated in many cellular processes. The enzyme is regulated at the post-translational level by an unusual system that includes antizymes (AZs) and antizyme inhibitors (AZINs). Most studies on this complex regulatory mechanism have been focused on human and rodent cells， showing that AZINs (AZIN1 and AZIN2) are homologues of ODC but devoid of enzymatic activity. Little is known about Xenopus ODC and its paralogues， in spite of the relevance of Xenopus as a model organism for biomedical research. We have used the information existing in different genomic databases to compare the functional properties... More
Ornithine decarboxylase (ODC) is a key enzyme in the biosynthesis of polyamines， organic cations that are implicated in many cellular processes. The enzyme is regulated at the post-translational level by an unusual system that includes antizymes (AZs) and antizyme inhibitors (AZINs). Most studies on this complex regulatory mechanism have been focused on human and rodent cells， showing that AZINs (AZIN1 and AZIN2) are homologues of ODC but devoid of enzymatic activity. Little is known about Xenopus ODC and its paralogues， in spite of the relevance of Xenopus as a model organism for biomedical research. We have used the information existing in different genomic databases to compare the functional properties of the amphibian ODC1， AZIN1 and AZIN2/ODC2， by means of transient transfection experiments of HEK293T cells. Whereas the properties of xlODC1 and xlAZIN1 were similar to those reported for their mammalian orthologues， the former catalyzing the decarboxylation of L-ornithine preferentially to that of L-lysine， xlAZIN2/xlODC2 showed important differences with respect to human and mouse AZIN2. xlAZIN2 did not behave as an antizyme inhibitor， but it rather acts as an authentic decarboxylase forming cadaverine， due to its higher affinity to L-lysine than to L-ornithine as substrate; so， in accordance with this， it should be named as lysine decarboxylase (LDC) or lysine/ornithine decarboxylase (LODC). In addition， AZ1 stimulated the degradation of xlAZIN2 by the proteasome， but the removal of the 21 amino acid C-terminal tail， with a sequence quite different to that of mouse or human ODC， made the protein resistant to degradation. Collectively， our results indicate that in Xenopus there is only one antizyme inhibitor (xlAZIN1) and two decarboxylases， xlODC1 and xlLDC， with clear preferences for L-ornithine and L-lysine， respectively.
