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Literature summary extracted from

  • Zhou, Y.; Ma, C.; Karmouch, J.; Arabi Katbi, H.; Liu, X.J.
    An anti-apoptotic role for ornithine decarboxylase during oocyte maturation (2009), Mol. Cell. Biol., 29, 1786-1795.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.17 progesterone ODC activity gradually increases in the presence of progesterone Xenopus laevis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.17 ODC expression analysis, overview Xenopus laevis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.17 additional information inhibition of ODC translation by antisense morpholino oligos, xODC mo, abolishes ODC activity increase during oocyte maturation Xenopus laevis

General Stability

EC Number General Stability Organism
4.1.1.17 ODC has a very short half-life Xenopus laevis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.17 alpha-difluoromethylornithine a highly specific suicide inhibitor of ODC causing complete, irreversible inhibition Xenopus laevis
4.1.1.17 antizyme ODC antizyme, a polyamine-induced protein, binds ODC, serving to inhibit ODC activity and to promote proteasome-mediated ODC degradation Xenopus laevis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.1.17 cytoplasm
-
 Xenopus laevis 5737
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.17 L-ornithine Xenopus laevis ODC is the rate-limiting enzyme in the cellular biosynthetic pathway to polyamines putrescine, spermidine and spermine. During mitotic cell cycle, ODC exhibits two activity peaks, one at G1/S transition and the second during G2/M transition, anti-apoptotic role for ornithine decarboxylase during oocyte maturation, overview putrescine + CO2
-
 ?
4.1.1.17 additional information Xenopus laevis ODC degradation is catalyzed by the 26S proteasome without prior polyubiquitination ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.17 Xenopus laevis
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.1.1.17 additional information during mitotic cell cycle, ODC exhibits two activity peaks, one at G1/S transition and the second during G2/M transition Xenopus laevis
-
4.1.1.17 oocyte
-
 Xenopus laevis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.17 L-ornithine
-
 Xenopus laevis putrescine + CO2
-
 ?
4.1.1.17 L-ornithine ODC is the rate-limiting enzyme in the cellular biosynthetic pathway to polyamines putrescine, spermidine and spermine. During mitotic cell cycle, ODC exhibits two activity peaks, one at G1/S transition and the second during G2/M transition, anti-apoptotic role for ornithine decarboxylase during oocyte maturation, overview Xenopus laevis putrescine + CO2
-
 ?
4.1.1.17 additional information ODC degradation is catalyzed by the 26S proteasome without prior polyubiquitination Xenopus laevis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.17 ODC
-
 Xenopus laevis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.17 37
-
 assay at Xenopus laevis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.17 7.4
-
 assay at Xenopus laevis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.17 pyridoxal 5'-phosphate
-
 Xenopus laevis