Recombinant human Ornithine Decarboxylase/ODC protein (Active)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Ornithine Decarboxylase also known as ODC or ODC1 is an enzyme that plays an important role in polyamine biosynthesis. This enzyme catalyzes the decarboxylation of ornithine to form putrescine a precursor for spermidine and spermine. ODC is a small protein with a molecular mass around 48 kDa. It is expressed in various tissues including the liver kidney and brain. ODC expression tends to be highest in rapidly growing tissues due to its involvement in cell growth and differentiation.

Biological function summary

ODC actively participates in cell proliferation and differentiation by regulating the levels of polyamines which are essential for DNA stabilization and cellular processes. While ODC does not form part of a larger protein complex its activity requires the presence of cofactor pyridoxal 5'-phosphate. By controlling polyamine synthesis ODC influences gene expression ion channel functions and protein synthesis impacting cell cycle progression and apoptosis.

Pathways

Ornithine decarboxylation connects with important biological processes such as the urea cycle and polyamine biosynthetic pathway. In these pathways enzymes like arginase and S-adenosylmethionine decarboxylase work closely with ODC. ODC's role in regulating polyamine levels makes it an important component of cellular metabolism and growth pathways. Through these pathways ODC coordinates with other proteins to ensure proper cellular function and response to growth signals.

ODC activity has been linked to cancer and neurological disorders. Overexpression and dysregulation of ODC can lead to increased polyamine levels which associate with tumor development and proliferation particularly in colorectal cancer. ODC also connects with proteins like c-Myc which regulates its expression and is often dysregulated in cancer. In neurological disorders abnormal ODC function affects neurodegeneration influencing proteins involved in neuronal survival and plasticity.