High impact information on odc-1

• We now show that when ODC-deficient worms are transferred to polyamine-free medium, they show a strong phenotype. odc-1 worms have two different fates, depending upon the developmental stage at which polyamines are removed [1].
• Supplementing deficient medium with the polyamine spermidine allows ODC-deficient worms to develop as on complex medium [1].
• Ornithine decarboxylase (ODC) catalyses the conversion of ornithine to putrescine, an obligate precursor to the polyamines spermidine and spermine [1].
• Together, these findings suggest that ODC activity is most critically required during oogenesis and embryogenesis and, furthermore, that exogenous polyamines can override the requirement for ODC activity [1].
• The mRNA is 1.5 kb in size and is formed by trans-splicing to SL1, a common 5' RNA segment. odc-1 maps to the middle of LG V, between dpy-11 and unc-42 and near a breakpoint of the nDf32 deficiency strain [2].

Biological context of odc-1

• The ornithine decarboxylase gene of Caenorhabditis elegans: cloning, mapping and mutagenesis [2].
• Functional amino acids are conserved, suggesting that the two active sites of the P. redivivus ODC are formed at the interface of a homodimer, as described for mammalian ODCs [3].

Associations of odc-1 with chemical compounds

• Agmatine, putrescine, spermidine and spermine inhibit ornithine decarboxylase in a non-competitive manner with Ki values of 10, 53.5, 59 and 855 microM respectively [4].
• Unlike previously described ornithine decarboxylases, the enzyme activity is membrane-associated and remains in the membrane fraction after treatment with high salt, detergents or phosphatidylinositol-specific phospholipase C. Ornithine has an apparent Km value of 2.7 microM for ornithine decarboxylase [4].

Other interactions of odc-1

• In Caenorhabditis elegans the polyamine synthetic pathway consists of three enzymes, ornithine decarboxylase (ODC), S-adenosylmethionine decarboxylase (AdoMetDC) and spermidine synthase [5].

Analytical, diagnostic and therapeutic context of odc-1

• Molecular cloning and characterization of ornithine decarboxylase cDNA of the nematode Panagrellus redivivus [3].
• In a PCR with degenerate primers encoding highly conserved amino acids within ornithine decarboxylases (ODCs) of several organisms, a fragment of the ODC gene of the free-living nematode Panagrellus redivivus was isolated [3].

References