Wikipedia

OAZ1

Ornithine decarboxylase antizyme is an enzyme that in humans is encoded by the OAZ1 gene.[5][6][7]

OAZ1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesOAZ1, AZI, OAZ, ornithine decarboxylase antizyme 1, AZ1
External IDsOMIM: 601579; MGI: 109433; HomoloGene: 7455; GeneCards: OAZ1; OMA:OAZ1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

4946

18245

Ensembl

ENSG00000104904

ENSMUSG00000035242

UniProt

P54368

P54369

RefSeq (mRNA)

NM_004152
NM_001301020

NM_001301034
NM_008753

RefSeq (protein)

NP_001287949
NP_004143

NP_001287963
NP_032779

Location (UCSC)Chr 19: 2.27 – 2.27 MbChr 10: 80.66 – 80.67 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[7]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000104904 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035242 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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 7811704.293-5&rft.date=1995-02&rft_id=info:doi/10.1016/0167-4838(94)90199-6&rft_id=info:pmid/7811704&rft.aulast=Tewari&rft.aufirst=DS&rft.au=Qian, Y&rft.au=Thornton, RD&rft.au=Pieringer, J&rft.au=Taub, R&rft.au=Mochan, E&rft.au=Tewari, M&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  6. ^ 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 8954789.102-104&rft.date=1997-03&rft_id=info:doi/10.1006/geno.1996.0601&rft_id=info:pmid/8954789&rft.aulast=Matsufuji&rft.aufirst=S&rft.au=Inazawa, J&rft.au=Hayashi, T&rft.au=Miyazaki, Y&rft.au=Ichiba, T&rft.au=Furusaka, A&rft.au=Matsufuji, T&rft.au=Atkins, JF&rft.au=Gesteland, RF&rft.au=Murakami, Y&rft.au=Hayashi, S&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  7. ^ a b "Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1".

Further reading

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  • Coffino P (2000). "Polyamines in spermiogenesis: not now, darling". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4421–4423. Bibcode:2000PNAS...97.4421C. doi:10.1073/pnas.97.9.4421. PMC 34313. PMID 10781034.4421-4423&rft.date=2000&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC34313#id-name=PMC&rft_id=info:pmid/10781034&rft_id=info:doi/10.1073/pnas.97.9.4421&rft_id=info:bibcode/2000PNAS...97.4421C&rft.au=Coffino P&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC34313&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 2724368.57-64&rft.date=1989&rft_id=info:doi/10.1080/15287398909531278&rft_id=info:pmid/2724368&rft.au=Savage RE&rft.au=Nofzinger K&rft.au=Bedell C&rft.au=Deangelo, Anthony&rft.au=Pereira, Michael&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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. PMC 7133313. PMID 7813017.51-60&rft.date=1995&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7133313#id-name=PMC&rft_id=info:pmid/7813017&rft_id=info:doi/10.1016/0092-8674(95)90450-6&rft.au=Matsufuji S&rft.au=Matsufuji T&rft.au=Miyazaki Y&rft.au=Murakami, Y&rft.au=Atkins, JF&rft.au=Gesteland, RF&rft.au=Hayashi, S&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7133313&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 8001569.547-554&rft.date=1995&rft_id=info:doi/10.1111/j.1432-1033.1994.tb20079.x&rft_id=info:pmid/8001569&rft.au=Mamroud-Kidron E&rft.au=Omer-Itsicovich M&rft.au=Bercovich Z&rft.au=Tobias, Karin E.&rft.au=Rom, Eran&rft.au=Kahana, Chaim&rft_id=https://doi.org/10.1111%2Fj.1432-1033.1994.tb20079.x&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 8185631.1721-1727&rft.date=1994&rft_id=info:doi/10.1006/bbrc.1994.1651&rft_id=info:pmid/8185631&rft.au=Ichiba T&rft.au=Matsufuji S&rft.au=Miyazaki Y&rft.au=Murakami, Y&rft.au=Tanaka, K&rft.au=Ichihara, A&rft.au=Hayashi, S&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • Yang D, Takii T, Hayashi H, et al. (1997). "Molcecular cloning of human antizyme cDNA". Biochem. Mol. Biol. Int. 38 (5): 957–64. PMID 9132164.957-64&rft.date=1997&rft_id=info:pmid/9132164&rft.au=Yang D&rft.au=Takii T&rft.au=Hayashi H&rft.au=Itoh, S&rft.au=Hayashi, M&rft.au=Onozaki, K&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 9426243.131-139&rft.date=1998&rft_id=info:doi/10.1016/S0378-1119(97)00504-0&rft_id=info:pmid/9426243&rft.aulast=Hayashi&rft.aufirst=T&rft.au=Matsufuji, S&rft.au=Hayashi, S&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 10473601.26425-26430&rft.date=1999&rft_id=info:doi/10.1074/jbc.274.37.26425&rft_id=info:pmid/10473601&rft.aulast=Zhu&rft.aufirst=C&rft.au=Lang, DW&rft.au=Coffino, P&rft_id=https://doi.org/10.1074%2Fjbc.274.37.26425&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 12359729.45957-45961&rft.date=2003&rft_id=info:doi/10.1074/jbc.M206799200&rft_id=info:pmid/12359729&rft.aulast=Chen&rft.aufirst=H&rft.au=MacDonald, A&rft.au=Coffino, P&rft_id=https://doi.org/10.1074%2Fjbc.M206799200&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 12426106.183-193&rft.date=2003&rft_id=info:doi/10.1016/S0378-1119(02)00978-2&rft_id=info:pmid/12426106&rft.au=Ike A&rft.au=Yamada S&rft.au=Tanaka H&rft.au=Nishimune, Y&rft.au=Nozaki, M&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.16899-16903&rft.date=2003&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241#id-name=PMC&rft_id=info:pmid/12477932&rft_id=info:doi/10.1073/pnas.242603899&rft_id=info:bibcode/2002PNAS...9916899M&rft.au=Strausberg RL&rft.au=Feingold EA&rft.au=Grouse LH&rft.au=Derge, JG&rft.au=Klausner, RD&rft.au=Collins, FS&rft.au=Wagner, L&rft.au=Shenmen, CM&rft.au=Schuler, GD&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature. 428 (6982): 529–535. Bibcode:2004Natur.428..529G. doi:10.1038/nature02399. PMID 15057824.529-535&rft.date=2004&rft_id=info:pmid/15057824&rft_id=info:doi/10.1038/nature02399&rft_id=info:bibcode/2004Natur.428..529G&rft.au=Grimwood J&rft.au=Gordon LA&rft.au=Olsen A&rft.au=Terry, Astrid&rft.au=Schmutz, Jeremy&rft.au=Lamerdin, Jane&rft.au=Hellsten, Uffe&rft.au=Goodstein, David&rft.au=Couronne, Olivier&rft_id=https://doi.org/10.1038%2Fnature02399&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 15355308.21-8&rft.date=2005&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134669#id-name=PMC&rft_id=info:pmid/15355308&rft_id=info:doi/10.1042/BJ20040547&rft.aulast=Mangold&rft.aufirst=U&rft.au=Leberer, E&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134669&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 15670771.206-212&rft.date=2005&rft_id=info:doi/10.1016/j.bbrc.2004.11.172&rft_id=info:pmid/15670771&rft.au=Choi KS&rft.au=Suh YH&rft.au=Kim WH&rft.au=Lee, T&rft.au=Jung, M&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 16373339.5277-5287&rft.date=2006&rft_id=info:doi/10.1074/jbc.M510004200&rft_id=info:pmid/16373339&rft.au=Ku M&rft.au=Howard S&rft.au=Ni W&rft.au=Lagna, G&rft.au=Hata, A&rft_id=https://doi.org/10.1074%2Fjbc.M510004200&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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. S2CID 13709685.801-814&rft.date=2006&rft_id=https://api.semanticscholar.org/CorpusID:13709685#id-name=S2CID&rft_id=info:pmid/16713569&rft_id=info:doi/10.1016/j.cell.2006.03.032&rft.au=Lim J&rft.au=Hao T&rft.au=Shaw C&rft.au=Patel, Akash J.&rft.au=Szabó, Gábor&rft.au=Rual, Jean-François&rft.au=Fisk, C. Joseph&rft.au=Li, Ning&rft.au=Smolyar, Alex&rft_id=https://doi.org/10.1016%2Fj.cell.2006.03.032&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">
  • 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 17630775.8920-8932&rft.date=2007&rft_id=info:doi/10.1021/bi7000328&rft_id=info:pmid/17630775&rft.au=Tsuji T&rft.au=Katsurano M&rft.au=Ibaragi S&rft.au=Shima, Kaori&rft.au=Sasaki, Akira&rft.au=Hu, Guo-fu&rfr_id=info:sid/en.wikipedia.org:OAZ1" class="Z3988">


 

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