Ornithine decarboxylase 1 (ODC1) (ODC1)

Ornithine decarboxylase 1 (ODC1) is a pyridoxal phosphate-dependent enzyme that catalyzes the decarboxylation of L-ornithine to putrescine, representing the first and rate-limiting step in polyamine biosynthesis (UniProt: P11926). Polyamines such as putrescine, spermidine, and spermine are essential for fundamental cellular processes, including DNA replication, protein synthesis, and cell proliferation (ResearchGate, 2025). ODC1 is highly regulated at the transcriptional, translational, and post-translational levels, including rapid degradation by the 26S proteasome via antizyme binding (Wikipedia). Dysregulation of ODC1 is a hallmark of many hyperproliferative diseases; it is a direct transcriptional target of the MYC oncogene and is frequently overexpressed in various cancers, including neuroblastoma and colorectal cancer (NIH: PMC7994084). Pharmacological inhibition of ODC1 by eflornithine (DFMO), an irreversible suicide inhibitor, has been successfully employed in the treatment of African trypanosomiasis and is currently being investigated for cancer chemoprevention and the treatment of Bachmann-Bupp syndrome, a rare genetic disorder caused by ODC1 gain-of-function mutations (NIH: PMC7994084; PubMed: 1438532).

Other names

Ornithine decarboxylaseODCODC-1

Irreversible inhibition of ornithine decarboxylase (suicide inhibition), leading to the depletion of intracellular polyamines (putrescine, spermidine, and spermine) and subsequent arrest of cell growth (PubMed: 1438532; UniProt: P11926).