OAZ1

Ornithine decarboxylase antizyme 1
Identifiers
SymbolsOAZ1 ; AZI; OAZ
External IDsOMIM: 601579 MGI: 109433 HomoloGene: 7455 GeneCards: OAZ1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez494618245
EnsemblENSG00000104904ENSMUSG00000035242
UniProtP54368P54369
RefSeq (mRNA)NM_001301020NM_001301034
RefSeq (protein)NP_001287949NP_001287963
Location (UCSC)Chr 19:
2.27 – 2.27 Mb		Chr 10:
80.83 – 80.83 Mb
PubMed search

Ornithine decarboxylase antizyme is an enzyme that in humans is encoded by the OAZ1 gene.[1][2][3]

Ornithine decarboxylase catalyzes the conversion of ornithine to putrescine in the first and apparently rate-limiting step in polyamine biosynthesis. The ornithine decarboxylase antizymes play a role in the regulation of polyamine synthesis by binding to and inhibiting ornithine decarboxylase. Antizyme expression is auto-regulated by polyamine-enhanced translational frameshifting. The antizyme encoded by this gene inhibits ornithine decarboxylase and accelerates its degradation.[3]

References

  1. ↑ Tewari DS, Qian Y, Thornton RD, Pieringer J, Taub R, Mochan E, Tewari M (Feb 1995). "Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme". Biochim Biophys Acta 1209 (2): 293–5. doi:10.1016/0167-4838(94)90199-6. PMID 7811704.
  2. ↑ Matsufuji S, Inazawa J, Hayashi T, Miyazaki Y, Ichiba T, Furusaka A, Matsufuji T, Atkins JF, Gesteland RF, Murakami Y, Hayashi S (Mar 1997). "Assignment of the human antizyme gene (OAZ) to chromosome 19p13.3 by fluorescence in situ hybridization". Genomics 38 (1): 102–104. doi:10.1006/geno.1996.0601. PMID 8954789.
  3. ↑ 3.0 3.1 "Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1".

Further reading

  • Coffino P (2000). "Polyamines in spermiogenesis: not now, darling". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4421–4423. doi:10.1073/pnas.97.9.4421. PMC 34313. PMID 10781034.
  • Savage RE; Nofzinger K; Bedell C et al. (1989). "Chloroform-induced multiple forms of ornithine decarboxylase: differential sensitivity of forms to enhancement by diethyl maleate and inhibition by ODC-antizyme". Journal of toxicology and environmental health 27 (1): 57–64. doi:10.1080/15287398909531278. PMID 2724368.
  • Matsufuji S; Matsufuji T; Miyazaki Y et al. (1995). "Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme". Cell 80 (1): 51–60. doi:10.1016/0092-8674(95)90450-6. PMID 7813017.
  • Mamroud-Kidron E; Omer-Itsicovich M; Bercovich Z et al. (1995). "A unified pathway for the degradation of ornithine decarboxylase in reticulocyte lysate requires interaction with the polyamine-induced protein, ornithine decarboxylase antizyme". Eur. J. Biochem. 226 (2): 547–554. doi:10.1111/j.1432-1033.1994.tb20079.x. PMID 8001569.
  • Ichiba T; Matsufuji S; Miyazaki Y et al. (1994). "Functional regions of ornithine decarboxylase antizyme". Biochem. Biophys. Res. Commun. 200 (3): 1721–1727. doi:10.1006/bbrc.1994.1651. PMID 8185631.
  • Yang D; Takii T; Hayashi H et al. (1997). "Molcecular cloning of human antizyme cDNA". Biochem. Mol. Biol. Int. 38 (5): 957–64. PMID 9132164.
  • Hayashi T, Matsufuji S, Hayashi S (1998). "Characterization of the human antizyme gene". Gene 203 (2): 131–139. doi:10.1016/S0378-1119(97)00504-0. PMID 9426243.
  • Zhu C, Lang DW, Coffino P (1999). "Antizyme2 is a negative regulator of ornithine decarboxylase and polyamine transport". J. Biol. Chem. 274 (37): 26425–26430. doi:10.1074/jbc.274.37.26425. PMID 10473601.
  • Chen H, MacDonald A, Coffino P (2003). "Structural elements of antizymes 1 and 2 are required for proteasomal degradation of ornithine decarboxylase". J. Biol. Chem. 277 (48): 45957–45961. doi:10.1074/jbc.M206799200. PMID 12359729.
  • Ike A; Yamada S; Tanaka H et al. (2003). "Structure and promoter activity of the gene encoding ornithine decarboxylase antizyme expressed exclusively in haploid germ cells in testis (OAZt/Oaz3)". Gene 298 (2): 183–193. doi:10.1016/S0378-1119(02)00978-2. PMID 12426106.
  • Strausberg RL; Feingold EA; Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Grimwood J; Gordon LA; Olsen A et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature 428 (6982): 529–535. doi:10.1038/nature02399. PMID 15057824.
  • Mangold U, Leberer E (2005). "Regulation of all members of the antizyme family by antizyme inhibitor". Biochem. J. 385 (Pt 1): 21–8. doi:10.1042/BJ20040547. PMC 1134669. PMID 15355308.
  • Choi KS; Suh YH; Kim WH et al. (2005). "Stable siRNA-mediated silencing of antizyme inhibitor: regulation of ornithine decarboxylase activity". Biochem. Biophys. Res. Commun. 328 (1): 206–212. doi:10.1016/j.bbrc.2004.11.172. PMID 15670771.
  • Ku M; Howard S; Ni W et al. (2006). "OAZ regulates bone morphogenetic protein signaling through Smad6 activation". J. Biol. Chem. 281 (8): 5277–5287. doi:10.1074/jbc.M510004200. PMID 16373339.
  • Lim J; Hao T; Shaw C et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell 125 (4): 801–814. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
  • Tsuji T; Katsurano M; Ibaragi S et al. (2007). "Ornithine decarboxylase antizyme upregulates DNA-dependent protein kinase and enhances the nonhomologous end-joining repair of DNA double-strand breaks in human oral cancer cells". Biochemistry 46 (31): 8920–8932. doi:10.1021/bi7000328. PMID 17630775.