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Gene Review

AOS  -  allene oxide synthase

Arabidopsis thaliana

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Disease relevance of AOS


High impact information on AOS


Biological context of AOS


Associations of AOS with chemical compounds

  • The methyl esters of OPDA or JA (OPDAME, JAME) and coronatine, are strong inducers of AOS mRNA, polypeptide and enzymatic activity [11].
  • Salicylic acid (SA) was an inducer of AOS activity while abscisic acid (ABA) had no effect [11].
  • Our results also suggest that AOS expression is limiting JA levels in wounded plants, but that the AOS hydroperoxide substrate levels, controlled by upstream enzymes (lipoxygenase and phospholipase), determine JA levels in unwounded plants [6].
  • AOS uses hydroperoxylinolenic acid as an oxygen donor as well as the substrate, thus the biochemical conversion of 13(S)-hydroperoxylinolenic acid to allene oxide can proceed in the absence of oxygen and NADPH [1].
  • Among the derivatives prepared, heptyl 8-[1-(2,4-dichlorophenyl)-2-imidazolylethoxy]octanoate (k) was found to be the most potent inhibitor, with an IC(50) of 10+/-5 nM, which is 250,000-fold and 1,000,000-fold more potent than the known AOS inhibitors, acetylsalicyclic acid (2.5 mM) and ketoconazole (10 mM), respectively [1].

Other interactions of AOS


  1. Design and synthesis of novel imidazole derivatives as potent inhibitors of allene oxide synthase(CYP74). Oh, K., Murofushi, N. Bioorg. Med. Chem. (2002) [Pubmed]
  2. Oligogalacturonide-mediated induction of a gene involved in jasmonic acid synthesis in response to the cell-wall-degrading enzymes of the plant pathogen Erwinia carotovora. Norman, C., Vidal, S., Palva, E.T. Mol. Plant Microbe Interact. (1999) [Pubmed]
  3. The Crystal Structure of Arabidopsis thaliana Allene Oxide Cyclase: Insights into the Oxylipin Cyclization Reaction. Hofmann, E., Zerbe, P., Schaller, F. Plant Cell (2006) [Pubmed]
  4. A novel class of oxylipins, sn1-O-(12-oxophytodienoyl)-sn2-O-(hexadecatrienoyl)-monogalactosyl Diglyceride, from Arabidopsis thaliana. Stelmach, B.A., Müller, A., Hennig, P., Gebhardt, S., Schubert-Zsilavecz, M., Weiler, E.W. J. Biol. Chem. (2001) [Pubmed]
  5. An Arabidopsis mutant defective in jasmonate response is allelic to the auxin-signaling mutant axr1. Tiryaki, I., Staswick, P.E. Plant Physiol. (2002) [Pubmed]
  6. A knock-out mutation in allene oxide synthase results in male sterility and defective wound signal transduction in Arabidopsis due to a block in jasmonic acid biosynthesis. Park, J.H., Halitschke, R., Kim, H.B., Baldwin, I.T., Feldmann, K.A., Feyereisen, R. Plant J. (2002) [Pubmed]
  7. Structure and regulation of the Arabidopsis thaliana allene oxide synthase gene. Kubigsteltig, I., Laudert, D., Weiler, E.W. Planta (1999) [Pubmed]
  8. Nitric oxide is induced by wounding and influences jasmonic acid signaling in Arabidopsis thaliana. Huang, X., Stettmaier, K., Michel, C., Hutzler, P., Mueller, M.J., Durner, J. Planta (2004) [Pubmed]
  9. Evidence supporting a role of jasmonic acid in Arabidopsis leaf senescence. He, Y., Fukushige, H., Hildebrand, D.F., Gan, S. Plant Physiol. (2002) [Pubmed]
  10. The Arabidopsis male-sterile mutant dde2-2 is defective in the ALLENE OXIDE SYNTHASE gene encoding one of the key enzymes of the jasmonic acid biosynthesis pathway. von Malek, B., van der Graaff, E., Schneitz, K., Keller, B. Planta (2002) [Pubmed]
  11. Allene oxide synthase: a major control point in Arabidopsis thaliana octadecanoid signalling. Laudert, D., Weiler, E.W. Plant J. (1998) [Pubmed]
  12. Potato homologs of Arabidopsis thaliana genes functional in defense signaling--identification, genetic mapping, and molecular cloning. Pajerowska, K.M., Parker, J.E., Gebhardt, C. Mol. Plant Microbe Interact. (2005) [Pubmed]
  13. Allene oxide synthase from Arabidopsis thaliana (CYP74A1) exhibits dual specificity that is regulated by monomer-micelle association. Hughes, R.K., Belfield, E.J., Ashton, R., Fairhurst, S.A., Göbel, C., Stumpe, M., Feussner, I., Casey, R. FEBS Lett. (2006) [Pubmed]
  14. Effect of volatile methyl jasmonate on the oxylipin pathway in tobacco, cucumber, and arabidopsis. Avdiushko, S., Croft, K.P., Brown, G.C., Jackson, D.M., Hamilton-Kemp, T.R., Hildebrand, D. Plant Physiol. (1995) [Pubmed]
  15. Molecular characterization of an Arabidopsis gene encoding hydroperoxide lyase, a cytochrome P-450 that is wound inducible. Bate, N.J., Sivasankar, S., Moxon, C., Riley, J.M., Thompson, J.E., Rothstein, S.J. Plant Physiol. (1998) [Pubmed]
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