Literature summary for 4.1.1.17 extracted from

Ramos-Molina, B.; Lambertos, A.; Lopez-Contreras, A.J.; Penafiel, R.
Mutational analysis of the antizyme-binding element reveals critical residues for the function of ornithine decarboxylase (2013), Biochim. Biophys. Acta, 1830, 5157-5165.

Protein Variants

Protein Variants	Comment	Organism
A123S	mutation in a conserved residue of the antizyme-binding region, mutant is somehow more resistant to degradation than wild-type. About 130% of wild-type activity	Mus musculus
E138A	mutation in a conserved residue of the antizyme-binding region, mutant is degraded as efficientlyas wild-type. Almost complete loss of activity. Mutation diminishes the formation of enzyme dimers	Mus musculus
E138A/L139S	mutation prevents the degradation by the proteasome, complete loss of activity. Mutation diminishes the formation of enzyme dimers	Mus musculus
K115A	mutation in a conserved residue of the antizyme-binding region. About 30 of wild-type activity. Mutation diminishes the formation of enzyme dimers	Mus musculus
K115A/K141A	degradation by the proteasome occurs with similar efficiency as for wild-type. About 10% of wild-type activity. Mutation diminishes the formation of enzyme dimers	Mus musculus
K141A	mutation in a conserved residue of the antizyme-binding region. About 25% of wild-type activity	Mus musculus
L139A	mutation in a conserved residue of the antizyme-binding region, mutant is resistant to degradation. About 15% of wild-type activity. Mutation diminishes the formation of enzyme dimers	Mus musculus
L139S	mutation in a conserved residue of the antizyme-binding region, mutant is resistant to degradation. Almost complete loss of activity	Mus musculus

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-