The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

SPE1  -  ornithine decarboxylase SPE1

Saccharomyces cerevisiae S288c

Synonyms: ODC, ORD1, Ornithine decarboxylase, SPE10, YKL184W
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of SPE1

  • This cDNA was functionally expressed in strains of Escherichia coli and Saccharomyces cerevisiae that lack ODC and are dependent upon exogenous PA for survival [1].
  • Expression of MTAP in MTAP-deleted MCF-7 breast adenocarcinoma cells results in a significant reduction of ODC activity and reduction in polyamine levels [2].

High impact information on SPE1

  • Induction of neuronal differentiation and ornithine decarboxylase (ODCase) transcription by oncogenic p21N-ras does not occur in compactin-treated cells indicating that activity of oncogenic p21N-ras expressed in PC12 cells is abolished by compactin treatment [3].
  • As the cell density increases, there is a marked fall in the level of ornithine decarboxylase (ODC) in the MEU1(+) cells, which we show is caused by an antizyme-requiring degradation system [4].
  • [Subhi, A. L., et al. (2003) J. Biol. Chem. 278, 49868-49873] of a novel regulatory pathway in meu1Delta cells in which ODC is not responsive to spermidine [4].
  • The meu1Delta cells have a higher putrescine and a lower spermidine level than MEU1(+) cells, suggesting that the decreased spermidine level in the meu1Delta cultures is responsible for the greater apparent stability of ODC in the meu1Delta cells [4].
  • Molecular dynamics simulations have been used to derive the structures of ground (orotidine-5'-monophosphate decarboxylase x orotidine 5'-monophosphate; ODC x OMP) and intermediate (ODC x intermediate; ODC x I(-)) states in the ODC-catalyzed decarboxylation of OMP [5].

Chemical compound and disease context of SPE1


Biological context of SPE1


Anatomical context of SPE1


Associations of SPE1 with chemical compounds


Other interactions of SPE1

  • Since spe1 delta SPE2 cells can synthesize decarboxylated adenosylmethionine (dcAdoMet), these data indicate that dcAdoMet may be toxic to amine-deficient cells [17].
  • This suggests that ornithine decarboxylase activity is negatively controlled by the presence of spermidine aminopropyltransferase [9].
  • In both MEU1(+) and the meu1Delta cultures, the ODC levels were markedly decreased by the addition of spermidine to the media, and thus our results contradict the postulation of Subhi et al [4].
  • Saccharomyces cerevisiae strains were obtained by one-step gene replacement of a 900 bp fragment of the yeast ODC gene (SPE1) with the yeast URA3 gene [18].
  • However, the rest of the pathway including ornithine decarboxylase and spermidine synthase was probably inherited from bacterial genes present in the original host cell, common ancestor of plants and animals, that acquired the cyanobacterial endosymbiont [19].

Analytical, diagnostic and therapeutic context of SPE1


  1. Haemonchus contortus: cloning and functional expression of a cDNA encoding ornithine decarboxylase and development of a screen for inhibitors. Klein, R.D., Favreau, M.A., Alexander-Bowman, S.J., Nulf, S.C., Vanover, L., Winterrowd, C.A., Yarlett, N., Martinez, M., Keithly, J.S., Zantello, M.R., Thomas, E.M., Geary, T.G. Exp. Parasitol. (1997) [Pubmed]
  2. Methylthioadenosine phosphorylase regulates ornithine decarboxylase by production of downstream metabolites. Subhi, A.L., Diegelman, P., Porter, C.W., Tang, B., Lu, Z.J., Markham, G.D., Kruger, W.D. J. Biol. Chem. (2003) [Pubmed]
  3. ras isoprenylation is required for ras-induced but not for NGF-induced neuronal differentiation of PC12 cells. Qiu, M.S., Pitts, A.F., Winters, T.R., Green, S.H. J. Cell Biol. (1991) [Pubmed]
  4. Studies on the regulation of ornithine decarboxylase in yeast: effect of deletion in the MEU1 gene. Chattopadhyay, M.K., Tabor, C.W., Tabor, H. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  5. Molecular dynamic study of orotidine-5'-monophosphate decarboxylase in ground state and in intermediate state: a role of the 203-218 loop dynamics. Hur, S., Bruice, T.C. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  6. Two new photoaffinity polyamines appear to alter the helical twist of DNA in nucleosome core particles. Clark, E., Swank, R.A., Morgan, J.E., Basu, H., Matthews, H.R. Biochemistry (1991) [Pubmed]
  7. SPE1 and SPE2: two essential genes in the biosynthesis of polyamines that modulate +1 ribosomal frameshifting in Saccharomyces cerevisiae. Balasundaram, D., Dinman, J.D., Tabor, C.W., Tabor, H. J. Bacteriol. (1994) [Pubmed]
  8. Isolation and sequence of the gene encoding ornithine decarboxylase, SPE1, from Candida albicans by complementation of a spe1 delta strain of Saccharomyces cerevisiae. McNemar, M.D., Gorman, J.A., Buckley, H.R. Yeast (1997) [Pubmed]
  9. Regulatory mutations affecting ornithine decarboxylase activity in Saccharomyces cerevisiae. Cohn, M.S., Tabor, C.W., Tabor, H. J. Bacteriol. (1980) [Pubmed]
  10. Ornithine decarboxylase in Saccharomyces cerevisiae: chromosomal assignment and genetic mapping of the SPE1 gene. Xie, Q.W., Tabor, C.W., Tabor, H. Yeast (1990) [Pubmed]
  11. Effect of spermidine on the in vivo degradation of ornithine decarboxylase in Saccharomyces cerevisiae. Gupta, R., Hamasaki-Katagiri, N., White Tabor, C., Tabor, H. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  12. Regulation of Saccharomyces cerevisiae ornithine decarboxylase expression in response to polyamine. Fonzi, W.A. J. Biol. Chem. (1989) [Pubmed]
  13. The 20S proteasome mediates the degradation of mouse and yeast ornithine decarboxylase in yeast cells. Mamroud-Kidron, E., Rosenberg-Hasson, Y., Rom, E., Kahana, C. FEBS Lett. (1994) [Pubmed]
  14. Inhibition of the dimorphic transition of Candida albicans by the ornithine decarboxylase inhibitor 1,4-diaminobutanone: alterations in the glycoprotein composition of the cell wall. Martinez, J.P., Lopez-Ribot, J.L., Gil, M.L., Sentandreu, R., Ruiz-Herrera, J. J. Gen. Microbiol. (1990) [Pubmed]
  15. Mutants of Saccharomyces cerevisiae deficient in polyamine biosynthesis: studies on the regulation of ornithine decarboxylase. Tabor, C.W. Med. Biol. (1981) [Pubmed]
  16. Ornithine decarboxylase from Saccharomyces cerevisiae. Purification, properties, and regulation of activity. Tyagi, A.K., Tabor, C.W., Tabor, H. J. Biol. Chem. (1981) [Pubmed]
  17. The presence of an active S-adenosylmethionine decarboxylase gene increases the growth defect observed in Saccharomyces cerevisiae mutants unable to synthesize putrescine, spermidine, and spermine. Balasundaram, D., Xie, Q.W., Tabor, C.W., Tabor, H. J. Bacteriol. (1994) [Pubmed]
  18. A new model for disruption of the ornithine decarboxylase gene, SPE1, in Saccharomyces cerevisiae exhibits growth arrest and genetic instability at the MAT locus. Schwartz, B., Hittelman, A., Daneshvar, L., Basu, H.S., Marton, L.J., Feuerstein, B.G. Biochem. J. (1995) [Pubmed]
  19. The diverse bacterial origins of the Arabidopsis polyamine biosynthetic pathway. Illingworth, C., Mayer, M.J., Elliott, K., Hanfrey, C., Walton, N.J., Michael, A.J. FEBS Lett. (2003) [Pubmed]
  20. Measurement of the amount of ornithine decarboxylase in Saccharomyces cerevisiae and Saccharomyces uvarum by using alpha-[5-14C]difluoromethylornithine. Pösö, H., Pegg, A.E. Biochim. Biophys. Acta (1983) [Pubmed]
  21. Expression of the gene for ornithine decarboxylase of Saccharomyces cerevisiae in Escherichia coli. Fonzi, W.A., Sypherd, P.S. Mol. Cell. Biol. (1985) [Pubmed]
  22. The ornithine decarboxylase gene from Candida albicans. Sequence analysis and expression during dimorphism. López, M.C., García, S., Ruiz-Herrera, J., Domínguez, A. Curr. Genet. (1997) [Pubmed]
WikiGenes - Universities